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class="data">1</p></div></a><span><div class="stat-container"><p class="label"><span class="js-profile-total-view-text">Public Views</span></p><p class="data"><span class="js-profile-view-count"></span></p></div></span></div><div class="ri-section"><div class="ri-section-header"><span>Interests</span></div><div class="ri-tags-container"><a data-click-track="profile-user-info-expand-research-interests" data-has-card-for-ri-list="5187356" href="https://www.academia.edu/Documents/in/Oxidative_Stress"><div id="js-react-on-rails-context" style="display:none" data-rails-context="{"inMailer":false,"i18nLocale":"en","i18nDefaultLocale":"en","href":"https://independent.academia.edu/AsrulFuad","location":"/AsrulFuad","scheme":"https","host":"independent.academia.edu","port":null,"pathname":"/AsrulFuad","search":null,"httpAcceptLanguage":null,"serverSide":false}"></div> <div class="js-react-on-rails-component" style="display:none" data-component-name="Pill" 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class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/115474102/Construction_of_gene_fusion_of_anti_EGFRvIII_scFv_with_HPR_mut_gene_for_development_of_anti_cancer_drug_delivery_system"><img alt="Research paper thumbnail of Construction of gene fusion of anti-EGFRvIII scFv with HPR-mut gene for development of anti cancer drug delivery system" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/115474102/Construction_of_gene_fusion_of_anti_EGFRvIII_scFv_with_HPR_mut_gene_for_development_of_anti_cancer_drug_delivery_system">Construction of gene fusion of anti-EGFRvIII scFv with HPR-mut gene for development of anti cancer drug delivery system</a></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="115474102"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="115474102"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 115474102; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=115474102]").text(description); 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})(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=115474102]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":115474102,"title":"Construction of gene fusion of anti-EGFRvIII scFv with HPR-mut gene for development of anti cancer drug delivery 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$a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322619"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322619/Expression_of_recombinant_human_granulocyte_colony_stimulating_factor_in_Escherichia_coli_using_various_induction_methods"><img alt="Research paper thumbnail of Expression of recombinant human granulocyte-colony stimulating factor in Escherichia coli using various induction methods" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322619/Expression_of_recombinant_human_granulocyte_colony_stimulating_factor_in_Escherichia_coli_using_various_induction_methods">Expression of recombinant human granulocyte-colony stimulating factor in Escherichia coli using various induction methods</a></div><div class="wp-workCard_item"><span>IOP conference series</span><span>, Feb 1, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Granulocyte-colony stimulating factor (G-CSF) is a glycoprotein that has several therapeutic appl...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Granulocyte-colony stimulating factor (G-CSF) is a glycoprotein that has several therapeutic applications. It consists of 174 amino acids and manufactured by recombinant DNA technology. Until now, the Escherichia coli expression system is still become the first choice for producing recombinant proteins. It is because of this organism is simple to culture in low-cost medium and easy to scale up. In the course to find the most efficient way to produce a high yield of recombinant human G-CSF, we compared several types of medium with different induction methods. In this experiment, recombinant E. coli NiCo21(DE3) harbouring gene encoding rh-GCSF proteins were cultured in various media including auto-induction, non-induction, and IPTG-induction. To determine the protein expression profile, culture sampling was done every 12 h (up to 60 h). Then, the optical density at ʎ 600 nm was measured using UV spectrophotometer and rh-GCSF protein expression were characterized using SDS-PAGE and western blot analyses. ImageJ software was used to calculate the amount of rh-GCSF protein yield using Bovine Serum Albumin (BSA) with known concentration as a standard. Result of this experiment concluded that simple auto-induction medium from Imperial College could produce good amount of rh-GCSF proteins (117 µg/mL) with relatively low production cost and short incubation time.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322619"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322619"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322619; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322619]").text(description); $(".js-view-count[data-work-id=108322619]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322619; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322619']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322619, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=108322619]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322619,"title":"Expression of recombinant human granulocyte-colony stimulating factor in Escherichia coli using various induction methods","translated_title":"","metadata":{"abstract":"Granulocyte-colony stimulating factor (G-CSF) is a glycoprotein that has several therapeutic applications. It consists of 174 amino acids and manufactured by recombinant DNA technology. Until now, the Escherichia coli expression system is still become the first choice for producing recombinant proteins. It is because of this organism is simple to culture in low-cost medium and easy to scale up. In the course to find the most efficient way to produce a high yield of recombinant human G-CSF, we compared several types of medium with different induction methods. In this experiment, recombinant E. coli NiCo21(DE3) harbouring gene encoding rh-GCSF proteins were cultured in various media including auto-induction, non-induction, and IPTG-induction. To determine the protein expression profile, culture sampling was done every 12 h (up to 60 h). Then, the optical density at ʎ 600 nm was measured using UV spectrophotometer and rh-GCSF protein expression were characterized using SDS-PAGE and western blot analyses. ImageJ software was used to calculate the amount of rh-GCSF protein yield using Bovine Serum Albumin (BSA) with known concentration as a standard. Result of this experiment concluded that simple auto-induction medium from Imperial College could produce good amount of rh-GCSF proteins (117 µg/mL) with relatively low production cost and short incubation time.","publisher":"IOP Publishing","publication_date":{"day":1,"month":2,"year":2020,"errors":{}},"publication_name":"IOP conference series"},"translated_abstract":"Granulocyte-colony stimulating factor (G-CSF) is a glycoprotein that has several therapeutic applications. It consists of 174 amino acids and manufactured by recombinant DNA technology. Until now, the Escherichia coli expression system is still become the first choice for producing recombinant proteins. It is because of this organism is simple to culture in low-cost medium and easy to scale up. In the course to find the most efficient way to produce a high yield of recombinant human G-CSF, we compared several types of medium with different induction methods. In this experiment, recombinant E. coli NiCo21(DE3) harbouring gene encoding rh-GCSF proteins were cultured in various media including auto-induction, non-induction, and IPTG-induction. To determine the protein expression profile, culture sampling was done every 12 h (up to 60 h). Then, the optical density at ʎ 600 nm was measured using UV spectrophotometer and rh-GCSF protein expression were characterized using SDS-PAGE and western blot analyses. ImageJ software was used to calculate the amount of rh-GCSF protein yield using Bovine Serum Albumin (BSA) with known concentration as a standard. Result of this experiment concluded that simple auto-induction medium from Imperial College could produce good amount of rh-GCSF proteins (117 µg/mL) with relatively low production cost and short incubation time.","internal_url":"https://www.academia.edu/108322619/Expression_of_recombinant_human_granulocyte_colony_stimulating_factor_in_Escherichia_coli_using_various_induction_methods","translated_internal_url":"","created_at":"2023-10-18T18:12:06.076-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Expression_of_recombinant_human_granulocyte_colony_stimulating_factor_in_Escherichia_coli_using_various_induction_methods","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":2639492,"name":"IOP conference series-MSE","url":"https://www.academia.edu/Documents/in/IOP_conference_series-MSE"}],"urls":[{"id":34836664,"url":"https://doi.org/10.1088/1755-1315/439/1/012042"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322618"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322618/Optimization_of_expression_JTAT_protein_with_emphasis_on_transformation_efficiency_and_IPTG_concentration"><img alt="Research paper thumbnail of Optimization of expression JTAT protein with emphasis on transformation efficiency and IPTG concentration" class="work-thumbnail" src="https://attachments.academia-assets.com/106737342/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322618/Optimization_of_expression_JTAT_protein_with_emphasis_on_transformation_efficiency_and_IPTG_concentration">Optimization of expression JTAT protein with emphasis on transformation efficiency and IPTG concentration</a></div><div class="wp-workCard_item"><span>Journal of Genetic Engineering and Biotechnology</span><span>, Dec 1, 2017</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="79e6fc996316153bcf4470e8c0b09b01" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737342,"asset_id":108322618,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737342/download_file?st=MTczMjU5Mjc1NCw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322618"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322618"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322618; 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This research was aimed to optimize the expression of Jembrana TAT (JTAT) protein with preparing Escherichia coli (E. coli) in advance using adopted methods of M1 (MgCl 2 + CaCl 2) and M2 (CaCl 2 + Glycerol). The best transformation efficiency resulting from a better transformation method was used to subsequent expression of JTAT protein. A synthetic tat gene encoding protein JTAT was previously cloned into pBT-hisC. Concentration of 200; 400; 600 mM IPTG was induced to a small volume culture (200 ml; OD 600 = 4), incubated for 3 h. Pellets were harvested by centrifugation (4000 rpm; 4°C; 15 min). Buffer B (10 mM Immidazole) was added into pellets, lysed by freeze-thaw followed by sonication. Supernatant was collected by centrifugation (10,000 rpm; 4°C; 20 min) and purified using Ni-NTA Agarose resin, released by elution buffer (E) containing 400 mM Immidazole to collect purified protein twice (E1, E2). The protein was characterized by SDS-PAGE and Western Blot (WB), quantified (at k595 nm) with BSA standard method in prior. The result showed that transformation efficiency was better in M2 (2.53 Â 10 6) than M1 (3.10 Â 10 5). The JTAT protein was expressed at a right size of 11.8 kDa. Concentration of 200 mM IPTG produced a significantly better protein yield (1.500 ± 0.089 mg/ml; P \u003c 0.05) than 600 mM IPTG (0.896 ± 0.052 mg/ml) and not different to 400 mM IPTG (1.298 ± 0.080 mg/ml). This research indicated that transformation efficiency needs to be taken account in prior of optimization of the protein expression.","publication_date":{"day":1,"month":12,"year":2017,"errors":{}},"publication_name":"Journal of Genetic Engineering and Biotechnology","grobid_abstract_attachment_id":106737342},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322618/Optimization_of_expression_JTAT_protein_with_emphasis_on_transformation_efficiency_and_IPTG_concentration","translated_internal_url":"","created_at":"2023-10-18T18:12:05.825-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737342,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737342/thumbnails/1.jpg","file_name":"main.PMC6296586.pdf","download_url":"https://www.academia.edu/attachments/106737342/download_file?st=MTczMjU5Mjc1NCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Optimization_of_expression_JTAT_protein.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737342/main.PMC6296586-libre.pdf?1697680287=\u0026response-content-disposition=attachment%3B+filename%3DOptimization_of_expression_JTAT_protein.pdf\u0026Expires=1732596354\u0026Signature=R4wG98bg~iS-QrlfOpKjkr5hu~-2s25CQDvpr3fO~52PXlzWl1j2okqUm4SaLWb7eDx4vDSMpbfk~zVKCUQsAtQk0nSY7jDa3rRctmSpc2hpNNDaPWp7VwfAprsQksfb7Ae6~v-5VBlKoN6fIESgnWsOKNFPPIA1WYd9NCDWV-cyhkUTt2-CxKM6W89cMWs9Uyv0LOO7imk9GBEHpVgM1kzQOmQowQzMgNcBIxyCcG5AKi6Bx3s1nSPpTC0cVAvhcW-gMhiK3MIH2jtZu4rev8n~EqN3h0syQXdmkAeIQV8X57JaQguJHl5t6UbYwRaCwS42XkyaXCHIBtlvTSmo1w__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Optimization_of_expression_JTAT_protein_with_emphasis_on_transformation_efficiency_and_IPTG_concentration","translated_slug":"","page_count":5,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737342,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737342/thumbnails/1.jpg","file_name":"main.PMC6296586.pdf","download_url":"https://www.academia.edu/attachments/106737342/download_file?st=MTczMjU5Mjc1NCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Optimization_of_expression_JTAT_protein.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737342/main.PMC6296586-libre.pdf?1697680287=\u0026response-content-disposition=attachment%3B+filename%3DOptimization_of_expression_JTAT_protein.pdf\u0026Expires=1732596354\u0026Signature=R4wG98bg~iS-QrlfOpKjkr5hu~-2s25CQDvpr3fO~52PXlzWl1j2okqUm4SaLWb7eDx4vDSMpbfk~zVKCUQsAtQk0nSY7jDa3rRctmSpc2hpNNDaPWp7VwfAprsQksfb7Ae6~v-5VBlKoN6fIESgnWsOKNFPPIA1WYd9NCDWV-cyhkUTt2-CxKM6W89cMWs9Uyv0LOO7imk9GBEHpVgM1kzQOmQowQzMgNcBIxyCcG5AKi6Bx3s1nSPpTC0cVAvhcW-gMhiK3MIH2jtZu4rev8n~EqN3h0syQXdmkAeIQV8X57JaQguJHl5t6UbYwRaCwS42XkyaXCHIBtlvTSmo1w__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":414331,"name":"Centrifugation","url":"https://www.academia.edu/Documents/in/Centrifugation"},{"id":482809,"name":"DICTIONARY OF BIOTECHNOLOGY AND GENETIC ENGINEERING","url":"https://www.academia.edu/Documents/in/DICTIONARY_OF_BIOTECHNOLOGY_AND_GENETIC_ENGINEERING"},{"id":960199,"name":"Sonication","url":"https://www.academia.edu/Documents/in/Sonication"},{"id":1256745,"name":"Lysis","url":"https://www.academia.edu/Documents/in/Lysis"}],"urls":[{"id":34836663,"url":"https://doi.org/10.1016/j.jgeb.2017.06.009"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322617"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322617/The_Effect_of_Growth_Condition_on_a_Soluble_Expression_of_Anti_EGFRvIII_Single_chain_Antibody_in_i_Escherichia_coli_i_NiCo21_DE3_"><img alt="Research paper thumbnail of The Effect of Growth Condition on a Soluble Expression of Anti-EGFRvIII Single-chain Antibody in <i>Escherichia coli</i> NiCo21(DE3)" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322617/The_Effect_of_Growth_Condition_on_a_Soluble_Expression_of_Anti_EGFRvIII_Single_chain_Antibody_in_i_Escherichia_coli_i_NiCo21_DE3_">The Effect of Growth Condition on a Soluble Expression of Anti-EGFRvIII Single-chain Antibody in <i>Escherichia coli</i> NiCo21(DE3)</a></div><div class="wp-workCard_item"><span>한국 미생물 생명공학회지</span><span>, Jun 28, 2021</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322617"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322617"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322617; 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The open reading frame of G-CSF was synthetically constructed in previous work and was codon optimized for best expression in E. coli. In this research, the gene was fused to thioredoxin (Trx) at the N-terminal in pET32 vector. The purpose of this research was to optimize the overproduction and purification processes to obtain high yield recombinant protein in soluble form, and to characterize the Trx-G-CSF fusion protein. Overproduction was performed using IPTG induction method for 3 and 6 hours. The protein was purified by Ni-NTA affinity chromatography and separated using gradient concentration of imidazole. The purified protein was then characterized by SDS-PAGE and Western Blot analysis. Further, enterokinase was used to separate G-CSF from the fusion protein. The purified form of G-CSF was subsequently characterized using Western Blot and mass spectrometry using MALDI-TOF. The results showed that the fusion protein was successfully produced in soluble part as much as 48.25% were obtained after 3 hours of induction. The yield of fusion protein was 67.37% from total protein (229.65 mg protein/L culture). The Western Blot analysis showed the G-CSF band at around 18.6 kDa. Mass spectrometry with MALDI-TOF/ TOF revealed that 25.86% of amino acid residue was recognized as part of human G-CSF sequence.","publication_date":{"day":22,"month":6,"year":2017,"errors":{}},"publication_name":"Annales Bogoriensis","grobid_abstract_attachment_id":106737341},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322616/Overproduction_and_Purification_of_Soluble_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_in_i_Escherichia_coli_i_Using_Thioredoxin_as_Fusion","translated_internal_url":"","created_at":"2023-10-18T18:12:05.376-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737341,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737341/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737341/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Overproduction_and_Purification_of_Solub.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737341/pdf-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DOverproduction_and_Purification_of_Solub.pdf\u0026Expires=1732596355\u0026Signature=ZKpTwFMPAGrWrv-bnq-sk~xgZjsBiIuz8jEJoe95-WX~MbEqGBsx4ZgIxbr~QlOfC0kduDJTsAzE3fk0AQGBn0Yi5XutANsb4aXSAbUu9hotxLQd7wKKEs3gL~-sa30M6oHwx3weS0yQQAoIPTiWTjLsUG1GeM5SFLeLRxO5xYajZV5Ig1epLjDt6wskPLGfgjsR7TBE3CmJy1QEncaw1oeg7FFCAWdTOzKieTfjvkAB5uZoVYzpQlaGf063t0zfpN~u5hg97cm08rRK3zekHxhElkTeVJItyBjlW6BuqExbw3XRSE4y9cY7ZHivJGCtxZRDa0DFYZqKZ3l0V349rw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Overproduction_and_Purification_of_Soluble_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_in_i_Escherichia_coli_i_Using_Thioredoxin_as_Fusion","translated_slug":"","page_count":8,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737341,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737341/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737341/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Overproduction_and_Purification_of_Solub.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737341/pdf-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DOverproduction_and_Purification_of_Solub.pdf\u0026Expires=1732596355\u0026Signature=ZKpTwFMPAGrWrv-bnq-sk~xgZjsBiIuz8jEJoe95-WX~MbEqGBsx4ZgIxbr~QlOfC0kduDJTsAzE3fk0AQGBn0Yi5XutANsb4aXSAbUu9hotxLQd7wKKEs3gL~-sa30M6oHwx3weS0yQQAoIPTiWTjLsUG1GeM5SFLeLRxO5xYajZV5Ig1epLjDt6wskPLGfgjsR7TBE3CmJy1QEncaw1oeg7FFCAWdTOzKieTfjvkAB5uZoVYzpQlaGf063t0zfpN~u5hg97cm08rRK3zekHxhElkTeVJItyBjlW6BuqExbw3XRSE4y9cY7ZHivJGCtxZRDa0DFYZqKZ3l0V349rw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":1159037,"name":"Fusion Protein","url":"https://www.academia.edu/Documents/in/Fusion_Protein"}],"urls":[{"id":34836661,"url":"https://doi.org/10.14203/ann.bogor.2017.v21.n1.1-8"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322615"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322615/Construction_and_Periplasmic_Expression_of_the_Anti_EGFRvIII_ScFv_Antibody_Gene_in_Escherichia_coli"><img alt="Research paper thumbnail of Construction and Periplasmic Expression of the Anti-EGFRvIII ScFv Antibody Gene in Escherichia coli" class="work-thumbnail" src="https://attachments.academia-assets.com/106737316/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322615/Construction_and_Periplasmic_Expression_of_the_Anti_EGFRvIII_ScFv_Antibody_Gene_in_Escherichia_coli">Construction and Periplasmic Expression of the Anti-EGFRvIII ScFv Antibody Gene in Escherichia coli</a></div><div class="wp-workCard_item"><span>Scientia Pharmaceutica</span><span>, 2016</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="59188f4cbd095636559481e76121fba2" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737316,"asset_id":108322615,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737316/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322615"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322615"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322615; 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H.","grobid_abstract":"In the previous study, we constructed an expression vector carrying the anti-EGFRvIII scFv antibody gene with V H-linker-V L orientation. The proteins were successfully produced in the periplasmic space of Escherichia coli. In this study, we substituted the inserted DNA with V L-linker-V H orientation of the anti-EGFRvIII scFv gene and analyzed its expression in E. coli. The DNA fragment was amplified from its cloning vector (pTz-rscFv), subsequently cloned into a previous expression vector containing the pelB signal sequence and his-tag, and then transformed into E. coli TOP10. The recombinant plasmids were characterized by restriction, PCR, and DNA sequencing analyses. The new anti-EGFRvIII scFv antibody proteins have been successfully expressed in the periplasmic compartment of E. coli Nico21(DE3) using 0.1 mM final concentration of IPTG induction. Total proteins, soluble periplasmic and cytoplasmic proteins, solubilized inclusion bodies, and extracellular proteins were analyzed by SDS-PAGE and Western Blot analyses. The results showed that soluble scFv proteins were found in all fractions except from the cytoplasmic space.","publication_date":{"day":null,"month":null,"year":2016,"errors":{}},"publication_name":"Scientia Pharmaceutica","grobid_abstract_attachment_id":106737316},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322615/Construction_and_Periplasmic_Expression_of_the_Anti_EGFRvIII_ScFv_Antibody_Gene_in_Escherichia_coli","translated_internal_url":"","created_at":"2023-10-18T18:12:05.117-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737316,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737316/thumbnails/1.jpg","file_name":"scipharm-84-00141.pdf","download_url":"https://www.academia.edu/attachments/106737316/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Construction_and_Periplasmic_Expression.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737316/scipharm-84-00141-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DConstruction_and_Periplasmic_Expression.pdf\u0026Expires=1732596355\u0026Signature=DMQxy2KHWv1F9aJ4tLDyBxOwuOOOCUY5A3AT8KLVRd8TzGmZolJVPU1lUi-8~BQRtfPtGPsK3AbBl8Ic73aarO-ROQEq9ZddZ8HqmZ8YlsrykG8XpJmpqOTWyos35Oa2jaoupkeCb8v3R7O0XUKjII4yDIhmjPquVbv73euwvzPnX3ScGswKyfM81InOvhmWp2GV5T~Swxw2XpazQ5VhP8OrzmsuOtJyTr16AoogYbXWJcBp2qyIssQO8ICdEfMCqmyqWU5v5rY4w5uxQN0bNDI1sddWMg-PYH4RanILvtWqaAtQaDfZsHJm6jDJF7urRUcJtoSAKkI8Q9qGj8b-qQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Construction_and_Periplasmic_Expression_of_the_Anti_EGFRvIII_ScFv_Antibody_Gene_in_Escherichia_coli","translated_slug":"","page_count":12,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737316,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737316/thumbnails/1.jpg","file_name":"scipharm-84-00141.pdf","download_url":"https://www.academia.edu/attachments/106737316/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Construction_and_Periplasmic_Expression.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737316/scipharm-84-00141-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DConstruction_and_Periplasmic_Expression.pdf\u0026Expires=1732596355\u0026Signature=DMQxy2KHWv1F9aJ4tLDyBxOwuOOOCUY5A3AT8KLVRd8TzGmZolJVPU1lUi-8~BQRtfPtGPsK3AbBl8Ic73aarO-ROQEq9ZddZ8HqmZ8YlsrykG8XpJmpqOTWyos35Oa2jaoupkeCb8v3R7O0XUKjII4yDIhmjPquVbv73euwvzPnX3ScGswKyfM81InOvhmWp2GV5T~Swxw2XpazQ5VhP8OrzmsuOtJyTr16AoogYbXWJcBp2qyIssQO8ICdEfMCqmyqWU5v5rY4w5uxQN0bNDI1sddWMg-PYH4RanILvtWqaAtQaDfZsHJm6jDJF7urRUcJtoSAKkI8Q9qGj8b-qQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":1114508,"name":"Plasmid","url":"https://www.academia.edu/Documents/in/Plasmid"},{"id":1159037,"name":"Fusion Protein","url":"https://www.academia.edu/Documents/in/Fusion_Protein"},{"id":1417742,"name":"Expression Vector","url":"https://www.academia.edu/Documents/in/Expression_Vector"}],"urls":[{"id":34836660,"url":"https://www.mdpi.com/2218-0532/84/1/141/pdf?version=1473211467"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322614"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322614/Heterologous_expression_of_Trichoderma_reesei_exoglucanase_Cel6A_in_Pichia_pastoris_under_the_control_of_GAP_promoter"><img alt="Research paper thumbnail of Heterologous expression of Trichoderma reesei exoglucanase (Cel6A) in Pichia pastoris under the control of GAP promoter" class="work-thumbnail" src="https://attachments.academia-assets.com/106737344/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322614/Heterologous_expression_of_Trichoderma_reesei_exoglucanase_Cel6A_in_Pichia_pastoris_under_the_control_of_GAP_promoter">Heterologous expression of Trichoderma reesei exoglucanase (Cel6A) in Pichia pastoris under the control of GAP promoter</a></div><div class="wp-workCard_item"><span>Nucleation and Atmospheric Aerosols</span><span>, 2019</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e7279f73ee5a6648a331f718ea390f89" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737344,"asset_id":108322614,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737344/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322614"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322614"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322614; 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dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "e7279f73ee5a6648a331f718ea390f89" } } $('.js-work-strip[data-work-id=108322614]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322614,"title":"Heterologous expression of Trichoderma reesei exoglucanase (Cel6A) in Pichia pastoris under the control of GAP promoter","translated_title":"","metadata":{"publisher":"American Institute of Physics","grobid_abstract":"Cellulolytic microorganisms produce several cellulase enzymes which have different specificities and modes of action. At least three types of cellulase (endo, exo, and β-glucosidase) are involved in the degradation of cellulose. One of them, exo-β-1,4 glucanase or cellobiohydrolase, can release either glucose or cellobiose from ends of cellulose chains. In this study, we tried to express an exoglucanase (Cel6A) gene heterologically in Pichia pastoris. The Cel6A gene was derived from Trichoderma reesei cellobiohydrolase 2 (CBH2). It was synthetically prepared, and codon optimized for best expression in yeast P. pastoris. The gene was placed under the regulation of the GAP promoter. The recombinant plasmid, named pLIPI-TrCel6A, inserted with T. reesei Cel6A (TrCel6A) gene has been integrated into P. pastoris SMD1168H genome, and the recombinant enzyme has been successfully expressed by P. pastoris with a major product showing a molecular size of around 50 kDa.","publication_date":{"day":null,"month":null,"year":2019,"errors":{}},"publication_name":"Nucleation and Atmospheric Aerosols","grobid_abstract_attachment_id":106737344},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322614/Heterologous_expression_of_Trichoderma_reesei_exoglucanase_Cel6A_in_Pichia_pastoris_under_the_control_of_GAP_promoter","translated_internal_url":"","created_at":"2023-10-18T18:12:04.901-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737344,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737344/thumbnails/1.jpg","file_name":"1.pdf","download_url":"https://www.academia.edu/attachments/106737344/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Heterologous_expression_of_Trichoderma_r.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737344/1-libre.pdf?1697680303=\u0026response-content-disposition=attachment%3B+filename%3DHeterologous_expression_of_Trichoderma_r.pdf\u0026Expires=1732596355\u0026Signature=gNluRZh95sm~Oc3YF6SfmN3B5ZP53-anQCotuwYJw0sMWC91hZaH57a8qZW9GzubDNAApxGYKE4NlOxAlQ36vja3Mehklpl28MoLiNkTb2Sd9mjYgcJf7fXSRiTauggjwCD8-GlNM8Tf0cA6aql~ukz6tuBLptsIVG9tgLIqWXZVSRugSv6sNo~5Wy3dyscxgM40d3Bll5f0IIdQylS3Zh~ihvKVRLi96MPYm2PqxXo9p~XPlFMRJc7oaHj8OGms02nGXSIBc4pmHNBXyOmg2V~UBdorxSe76ejvBQTRrBJhIUuR4D408X5OaLNIXsdVE2gyG1f0Ji-wCY3t7jjUVQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Heterologous_expression_of_Trichoderma_reesei_exoglucanase_Cel6A_in_Pichia_pastoris_under_the_control_of_GAP_promoter","translated_slug":"","page_count":10,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737344,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737344/thumbnails/1.jpg","file_name":"1.pdf","download_url":"https://www.academia.edu/attachments/106737344/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Heterologous_expression_of_Trichoderma_r.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737344/1-libre.pdf?1697680303=\u0026response-content-disposition=attachment%3B+filename%3DHeterologous_expression_of_Trichoderma_r.pdf\u0026Expires=1732596355\u0026Signature=gNluRZh95sm~Oc3YF6SfmN3B5ZP53-anQCotuwYJw0sMWC91hZaH57a8qZW9GzubDNAApxGYKE4NlOxAlQ36vja3Mehklpl28MoLiNkTb2Sd9mjYgcJf7fXSRiTauggjwCD8-GlNM8Tf0cA6aql~ukz6tuBLptsIVG9tgLIqWXZVSRugSv6sNo~5Wy3dyscxgM40d3Bll5f0IIdQylS3Zh~ihvKVRLi96MPYm2PqxXo9p~XPlFMRJc7oaHj8OGms02nGXSIBc4pmHNBXyOmg2V~UBdorxSe76ejvBQTRrBJhIUuR4D408X5OaLNIXsdVE2gyG1f0Ji-wCY3t7jjUVQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":43685,"name":"Cellulase","url":"https://www.academia.edu/Documents/in/Cellulase"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"},{"id":1398164,"name":"Trichoderma Reesei","url":"https://www.academia.edu/Documents/in/Trichoderma_Reesei"},{"id":2356118,"name":"Cellobiose","url":"https://www.academia.edu/Documents/in/Cellobiose"}],"urls":[{"id":34836659,"url":"https://doi.org/10.1063/1.5125548"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322613"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322613/Expression_and_characterization_of_Trichoderma_reesei_endoglucanase_II_in_Pichia_pastoris_under_the_regulation_of_the_GAP_promoter"><img alt="Research paper thumbnail of Expression and characterization of Trichoderma reesei endoglucanase II in Pichia pastoris under the regulation of the GAP promoter" class="work-thumbnail" src="https://attachments.academia-assets.com/106737315/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322613/Expression_and_characterization_of_Trichoderma_reesei_endoglucanase_II_in_Pichia_pastoris_under_the_regulation_of_the_GAP_promoter">Expression and characterization of Trichoderma reesei endoglucanase II in Pichia pastoris under the regulation of the GAP promoter</a></div><div class="wp-workCard_item"><span>Indonesian Journal of Biotechnology</span><span>, Dec 2, 2020</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ccb82b8fe82c545e12756eb44e30e5ee" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737315,"asset_id":108322613,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737315/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322613"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322613"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322613; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322613]").text(description); $(".js-view-count[data-work-id=108322613]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322613; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322613']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322613, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "ccb82b8fe82c545e12756eb44e30e5ee" } } $('.js-work-strip[data-work-id=108322613]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322613,"title":"Expression and characterization of Trichoderma reesei endoglucanase II in Pichia pastoris under the regulation of the GAP promoter","translated_title":"","metadata":{"publisher":"Gadjah Mada University","grobid_abstract":"Trichoderma reesei is known to be one of the organisms capable for producing various types of cellulase in high concentrations. Among these cellulases, the highest catalytic efficiency of endoglucanases II (EGII, EC 3.2.1.4) are considered important for industrial application. The characterization of the EGII is necessary since it is widely used in high-temperature reactions in the industries. In this study, the recombinant EGII protein was expressed in Pichia pastoris and it has a molecular mass of approximately 52 kDa. Recombinant EGII was purified using Ni-NTA affinity chromatography and characterized by SDS-PAGE and western blot analyses. The enzyme activity of recombinant EGII was measured using the Nelson Somogyi method to determine its optimum pH and temperature. The result showed that the maximum EGII expression was achieved after 72 h of culture incubation. The crude enzyme has optimum activity at pH 5.0, resulting in 16.3 U/mL and 14.6 U/mL activity at 40°C and 50°C, respectively. While the purified enzyme gave the specific activity of 115.7 U/mg under the optimum condition. Finally, our study demonstrated that recombinant EGII could retain the endoglucanase activity for 89% and 80% at 40°C and 50°C, respectively.","publication_date":{"day":2,"month":12,"year":2020,"errors":{}},"publication_name":"Indonesian Journal of Biotechnology","grobid_abstract_attachment_id":106737315},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322613/Expression_and_characterization_of_Trichoderma_reesei_endoglucanase_II_in_Pichia_pastoris_under_the_regulation_of_the_GAP_promoter","translated_internal_url":"","created_at":"2023-10-18T18:12:04.667-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737315,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737315/thumbnails/1.jpg","file_name":"29994.pdf","download_url":"https://www.academia.edu/attachments/106737315/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Expression_and_characterization_of_Trich.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737315/29994-libre.pdf?1697680314=\u0026response-content-disposition=attachment%3B+filename%3DExpression_and_characterization_of_Trich.pdf\u0026Expires=1732596355\u0026Signature=eVatdK8A0UEsWQuNagMSVDQUmxf7vpXytks69GxRzxZA6svm5G7hGPBdIHykfhcE593~SzdpphWoUEwaCisaI4iMql82AnFo3az1oLQkDRctVJ0L0DJvMbuY6wpHfPp09Cl~cNDk5MUtbWL4J0P0uNdpzvqpiAG4Fuovzl6znqJ-jZQ5fQTen1q4N9WY9XD0RyZZG7nqTyyegxJe2W1yZFG0OmbMDaUBIWh~PCzrMoxzjqB2B62fsqRpiye0nfzQ1-sa4NLJfTz2z7Lfnmk54hincnp78lCx63YVzZ~szOYfea~k68UXAHhQAwx63K-n7n04NLPdRpG~uV8FWxa0sQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Expression_and_characterization_of_Trichoderma_reesei_endoglucanase_II_in_Pichia_pastoris_under_the_regulation_of_the_GAP_promoter","translated_slug":"","page_count":8,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737315,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737315/thumbnails/1.jpg","file_name":"29994.pdf","download_url":"https://www.academia.edu/attachments/106737315/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Expression_and_characterization_of_Trich.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737315/29994-libre.pdf?1697680314=\u0026response-content-disposition=attachment%3B+filename%3DExpression_and_characterization_of_Trich.pdf\u0026Expires=1732596355\u0026Signature=eVatdK8A0UEsWQuNagMSVDQUmxf7vpXytks69GxRzxZA6svm5G7hGPBdIHykfhcE593~SzdpphWoUEwaCisaI4iMql82AnFo3az1oLQkDRctVJ0L0DJvMbuY6wpHfPp09Cl~cNDk5MUtbWL4J0P0uNdpzvqpiAG4Fuovzl6znqJ-jZQ5fQTen1q4N9WY9XD0RyZZG7nqTyyegxJe2W1yZFG0OmbMDaUBIWh~PCzrMoxzjqB2B62fsqRpiye0nfzQ1-sa4NLJfTz2z7Lfnmk54hincnp78lCx63YVzZ~szOYfea~k68UXAHhQAwx63K-n7n04NLPdRpG~uV8FWxa0sQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":43685,"name":"Cellulase","url":"https://www.academia.edu/Documents/in/Cellulase"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"},{"id":201241,"name":"Affinity chromatography","url":"https://www.academia.edu/Documents/in/Affinity_chromatography"},{"id":231661,"name":"Enzyme","url":"https://www.academia.edu/Documents/in/Enzyme"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":420864,"name":"Universitas Gadjah Mada","url":"https://www.academia.edu/Documents/in/Universitas_Gadjah_Mada"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":585595,"name":"Molecular Mass","url":"https://www.academia.edu/Documents/in/Molecular_Mass"},{"id":954401,"name":"Enzyme Assay","url":"https://www.academia.edu/Documents/in/Enzyme_Assay"},{"id":1398164,"name":"Trichoderma Reesei","url":"https://www.academia.edu/Documents/in/Trichoderma_Reesei"}],"urls":[{"id":34836658,"url":"https://jurnal.ugm.ac.id/ijbiotech/article/download/55604/29994"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322612"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322612/Transformation_of_recombinant_plasmid_pJ404_EGFRvIII_bfp_into_an_Escherichia_coli_NiCo21_DE3_expression_host_and_its_characterization"><img alt="Research paper thumbnail of Transformation of recombinant plasmid pJ404-EGFRvIII-bfp into an Escherichia coli NiCo21(DE3) expression host and its characterization" class="work-thumbnail" src="https://attachments.academia-assets.com/106737340/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322612/Transformation_of_recombinant_plasmid_pJ404_EGFRvIII_bfp_into_an_Escherichia_coli_NiCo21_DE3_expression_host_and_its_characterization">Transformation of recombinant plasmid pJ404-EGFRvIII-bfp into an Escherichia coli NiCo21(DE3) expression host and its characterization</a></div><div class="wp-workCard_item"><span>IOP conference series</span><span>, Apr 28, 2020</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="45f6677e9115186d09a4c94578ca809e" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737340,"asset_id":108322612,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737340/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322612"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322612"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322612; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322612]").text(description); $(".js-view-count[data-work-id=108322612]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322612; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322612']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322612, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "45f6677e9115186d09a4c94578ca809e" } } $('.js-work-strip[data-work-id=108322612]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322612,"title":"Transformation of recombinant plasmid pJ404-EGFRvIII-bfp into an Escherichia coli NiCo21(DE3) expression host and its characterization","translated_title":"","metadata":{"publisher":"IOP Publishing","grobid_abstract":"Epidermal growth factor receptor variant III (EGFRvIII) is a mutant of epidermal growth factor receptor (EGFR) that lacks 267 amino acids (exons 2-7) within its extracellular domain that results in the formation of a new epitope as a tumor specific target. A synthetic gene of EGFRvIII has been constructed by previous researchers to encode a fusion protein as a marker in targeted cancer therapies. This research was conducted to transform the recombinant plasmid pJ404-EGFRvIII into Escherichia coli NiCo21(DE3) host cells and characterize the E. coli NiCo21(DE3) transformants. Recombinant plasmid pJ404-EGFRvIII was isolated with an alkali lysis method and transformed into E. coli NiCo21(DE3) by heat-shock method. The transformants were grown on LB medium containing100 Ɋg/ml ampicillin and characterized by colony PCR method. The results showed that the pJ404-EGFRvIII recombinant plasmid was transformed successfully into E. coli NiCo21(DE3). With the result that, EGFRvIII gene might be express by E. coli NiCo21(DE3) for further analysis of protein expression and purification in tumor terapy.","publication_date":{"day":28,"month":4,"year":2020,"errors":{}},"publication_name":"IOP conference series","grobid_abstract_attachment_id":106737340},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322612/Transformation_of_recombinant_plasmid_pJ404_EGFRvIII_bfp_into_an_Escherichia_coli_NiCo21_DE3_expression_host_and_its_characterization","translated_internal_url":"","created_at":"2023-10-18T18:12:04.420-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737340,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737340/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737340/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Transformation_of_recombinant_plasmid_pJ.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737340/pdf-libre.pdf?1697680290=\u0026response-content-disposition=attachment%3B+filename%3DTransformation_of_recombinant_plasmid_pJ.pdf\u0026Expires=1732596355\u0026Signature=IhBkWxIp82v11K6IK-oAIauYn~tgKR~01XhwfQW8ruYGg9NLmDSM8fjN5K2WSOH08B2nV6t8bvSskzQpYgi6p4QOH4tbB-yTJUG8Jj1KAURvDOU6w~~HPR8NfNICuhF09AHKuwqhtQs0rMhWamUc7iyHeKNwppm2b-xObEeD2YHYVCeQdoWwaGbnKaVZE~YKH2SvdyCzbUCMuxCr~iL4oulKkIwbxPKFdDef4K5Jin1qf1Pui656AkNHPQlbc1HLK8R3~geJ2-CoRZQKjOV4tV7h-vxYVzMl9XHPftGVg4on3gmWGPldI13C5tbjWWkR2Zw8wz5fzTWemWdz6ZateA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Transformation_of_recombinant_plasmid_pJ404_EGFRvIII_bfp_into_an_Escherichia_coli_NiCo21_DE3_expression_host_and_its_characterization","translated_slug":"","page_count":5,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737340,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737340/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737340/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Transformation_of_recombinant_plasmid_pJ.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737340/pdf-libre.pdf?1697680290=\u0026response-content-disposition=attachment%3B+filename%3DTransformation_of_recombinant_plasmid_pJ.pdf\u0026Expires=1732596355\u0026Signature=IhBkWxIp82v11K6IK-oAIauYn~tgKR~01XhwfQW8ruYGg9NLmDSM8fjN5K2WSOH08B2nV6t8bvSskzQpYgi6p4QOH4tbB-yTJUG8Jj1KAURvDOU6w~~HPR8NfNICuhF09AHKuwqhtQs0rMhWamUc7iyHeKNwppm2b-xObEeD2YHYVCeQdoWwaGbnKaVZE~YKH2SvdyCzbUCMuxCr~iL4oulKkIwbxPKFdDef4K5Jin1qf1Pui656AkNHPQlbc1HLK8R3~geJ2-CoRZQKjOV4tV7h-vxYVzMl9XHPftGVg4on3gmWGPldI13C5tbjWWkR2Zw8wz5fzTWemWdz6ZateA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":159,"name":"Microbiology","url":"https://www.academia.edu/Documents/in/Microbiology"},{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":1114508,"name":"Plasmid","url":"https://www.academia.edu/Documents/in/Plasmid"},{"id":2639492,"name":"IOP conference series-MSE","url":"https://www.academia.edu/Documents/in/IOP_conference_series-MSE"}],"urls":[{"id":34836657,"url":"https://doi.org/10.1088/1755-1315/481/1/012009"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322611"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322611/Purification_of_recombinant_human_granulocyte_colony_stimulating_factor_from_Pichia_pastoris_using_two_ninta_chromatography_methods"><img alt="Research paper thumbnail of Purification of recombinant human granulocyte colony-stimulating factor from Pichia pastoris using two ninta chromatography methods" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322611/Purification_of_recombinant_human_granulocyte_colony_stimulating_factor_from_Pichia_pastoris_using_two_ninta_chromatography_methods">Purification of recombinant human granulocyte colony-stimulating factor from Pichia pastoris using two ninta chromatography methods</a></div><div class="wp-workCard_item"><span>IOP conference series</span><span>, Feb 22, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Human granulocyte colony-stimulating factor (hG-CSF) is a glycoprotein that stimulates the produc...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Human granulocyte colony-stimulating factor (hG-CSF) is a glycoprotein that stimulates the production of mature neutrophil and enhances its survival, proliferation, differentiation, and neutrofil precursor function. This study was carried out to determine the purity of recombinant protein employing two purification methods using NiNTA with imidazole and with pH gradient (without imidazole). The synthetic gene (gcsf-cmyc) was cloned into secretive expression vector pPICZαA and methanol utilizing alcohol oxidase (AOX1) promoters before being expressed in Pichia pastoris SMD1168H strain. The recombinant protein was purified using NiNTA chromatography with imidazole and pH gradient. All samples were analyzed using SDS PAGE, followed with detection using coomasie blue. The molecular mass of recombinant hG-CSF expressed in P. pastoris was ∼23kD. The efficiency of hG-CSF purification using NiNTA with imidazole was ∼63%, while with pH gradient was ∼89%. Purification techniques use pH gradients gradients can be applied to avoid used of imidazole, so that it does not contaminate protein samples.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322611"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322611"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322611; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322611]").text(description); $(".js-view-count[data-work-id=108322611]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322611; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322611']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322611, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=108322611]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322611,"title":"Purification of recombinant human granulocyte colony-stimulating factor from Pichia pastoris using two ninta chromatography methods","translated_title":"","metadata":{"abstract":"Human granulocyte colony-stimulating factor (hG-CSF) is a glycoprotein that stimulates the production of mature neutrophil and enhances its survival, proliferation, differentiation, and neutrofil precursor function. This study was carried out to determine the purity of recombinant protein employing two purification methods using NiNTA with imidazole and with pH gradient (without imidazole). The synthetic gene (gcsf-cmyc) was cloned into secretive expression vector pPICZαA and methanol utilizing alcohol oxidase (AOX1) promoters before being expressed in Pichia pastoris SMD1168H strain. The recombinant protein was purified using NiNTA chromatography with imidazole and pH gradient. All samples were analyzed using SDS PAGE, followed with detection using coomasie blue. The molecular mass of recombinant hG-CSF expressed in P. pastoris was ∼23kD. The efficiency of hG-CSF purification using NiNTA with imidazole was ∼63%, while with pH gradient was ∼89%. Purification techniques use pH gradients gradients can be applied to avoid used of imidazole, so that it does not contaminate protein samples.","publisher":"IOP Publishing","publication_date":{"day":22,"month":2,"year":2020,"errors":{}},"publication_name":"IOP conference series"},"translated_abstract":"Human granulocyte colony-stimulating factor (hG-CSF) is a glycoprotein that stimulates the production of mature neutrophil and enhances its survival, proliferation, differentiation, and neutrofil precursor function. This study was carried out to determine the purity of recombinant protein employing two purification methods using NiNTA with imidazole and with pH gradient (without imidazole). The synthetic gene (gcsf-cmyc) was cloned into secretive expression vector pPICZαA and methanol utilizing alcohol oxidase (AOX1) promoters before being expressed in Pichia pastoris SMD1168H strain. The recombinant protein was purified using NiNTA chromatography with imidazole and pH gradient. All samples were analyzed using SDS PAGE, followed with detection using coomasie blue. The molecular mass of recombinant hG-CSF expressed in P. pastoris was ∼23kD. The efficiency of hG-CSF purification using NiNTA with imidazole was ∼63%, while with pH gradient was ∼89%. Purification techniques use pH gradients gradients can be applied to avoid used of imidazole, so that it does not contaminate protein samples.","internal_url":"https://www.academia.edu/108322611/Purification_of_recombinant_human_granulocyte_colony_stimulating_factor_from_Pichia_pastoris_using_two_ninta_chromatography_methods","translated_internal_url":"","created_at":"2023-10-18T18:12:04.126-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Purification_of_recombinant_human_granulocyte_colony_stimulating_factor_from_Pichia_pastoris_using_two_ninta_chromatography_methods","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":4656,"name":"Chromatography","url":"https://www.academia.edu/Documents/in/Chromatography"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":605726,"name":"Imidazole","url":"https://www.academia.edu/Documents/in/Imidazole"},{"id":2639492,"name":"IOP conference series-MSE","url":"https://www.academia.edu/Documents/in/IOP_conference_series-MSE"}],"urls":[{"id":34836656,"url":"https://doi.org/10.1088/1755-1315/439/1/012044"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322609"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322609/Bioinformatics_Analysis_to_Construct_Cellulose_binding_Module_Synthetic_Gene_and_Design_Primer"><img alt="Research paper thumbnail of Bioinformatics Analysis to Construct Cellulose-binding Module Synthetic Gene and Design Primer" class="work-thumbnail" src="https://attachments.academia-assets.com/106737337/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322609/Bioinformatics_Analysis_to_Construct_Cellulose_binding_Module_Synthetic_Gene_and_Design_Primer">Bioinformatics Analysis to Construct Cellulose-binding Module Synthetic Gene and Design Primer</a></div><div class="wp-workCard_item"><span>Bioedukasi (Jember)</span><span>, Jul 31, 2019</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="6edddf573ef964d55086f637cea0a848" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737337,"asset_id":108322609,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737337/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322609"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322609"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322609; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322609]").text(description); $(".js-view-count[data-work-id=108322609]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322609; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322609']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322609, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "6edddf573ef964d55086f637cea0a848" } } $('.js-work-strip[data-work-id=108322609]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322609,"title":"Bioinformatics Analysis to Construct Cellulose-binding Module Synthetic Gene and Design Primer","translated_title":"","metadata":{"publisher":"UPT Penerbitan Universitas Jember","grobid_abstract":"Cellulose-binding module (CBM) is a protein domain commonly found in various types of cellulase enzymes. The function of this CBM can be used for the binding process and the immobilization of a protein in the cellulose matrix. CBM can be obtained from several organisms, one of them is Trichoderma reesei. To get a gene, it does not have to be isolated from the original organism. Gene sequences can be obtained synthetically through bioinformatics analysis in accordance with the same gene sequences as those at Gene Bank. Bioinformatics analysis can be used to find new gene sequences or existing genes. This study aims to get a cbmsyn synthetic gene quickly and efficiently without reducing protein activity, which can then be ligated with other genes so that it functions as an immobilized enzyme. From the results of bioinformatics analysis, obtained DNA sequences measuring around 498 pb with 166 amino acid protein lengths. The sequence was modified by adding several restriction sites, namely BamHI, AfeI, and ScaI. 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322607"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322607/The_Effect_Of_Temperature_On_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_Production_By_Pichia_pastoris_Expression_System"><img alt="Research paper thumbnail of The Effect Of Temperature On Recombinant Human Granulocyte Colony Stimulating Factor Production By Pichia pastoris Expression System" class="work-thumbnail" src="https://attachments.academia-assets.com/106737339/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322607/The_Effect_Of_Temperature_On_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_Production_By_Pichia_pastoris_Expression_System">The Effect Of Temperature On Recombinant Human Granulocyte Colony Stimulating Factor Production By Pichia pastoris Expression System</a></div><div class="wp-workCard_item"><span>INDONESIAN JOURNAL OF PHARMACY</span><span>, Jul 10, 2018</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="9c6cfda2a0d94c4825104733d8888c8e" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737339,"asset_id":108322607,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737339/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322607"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322607"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322607; 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The main objective of this work is to compare the effect of different temperature on the production of extracellular recombinant G-CSF in Pichia pastoris. Cells were cultured for 72h in baffled shake-flasks at 20°C, 25°C, and 30°C in two different medium; buffered glycerol/methanol-complex medium (BMGY/BMMY) and buffered minimal glycerol/methanol (BMGH/BMMH) after methanol induction every 12h. Expressed recombinant hG-CSF in the methylotrophic yeast P. pastoris was analyzed with SDS-PAGE. The 23 kDa protein was secreted into the culture supernatant when induced with methanol. Production of recombinant G-CSF protein in P. pastoris at 30°C at 48h incubation after methanol induction every 12h is the highest in both complex and minimum medium.","publication_date":{"day":10,"month":7,"year":2018,"errors":{}},"publication_name":"INDONESIAN JOURNAL OF PHARMACY","grobid_abstract_attachment_id":106737339},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322607/The_Effect_Of_Temperature_On_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_Production_By_Pichia_pastoris_Expression_System","translated_internal_url":"","created_at":"2023-10-18T18:12:03.601-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737339,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737339/thumbnails/1.jpg","file_name":"e2d4189d3b3a28da5a2e43068583b683506e.pdf","download_url":"https://www.academia.edu/attachments/106737339/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"The_Effect_Of_Temperature_On_Recombinant.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737339/e2d4189d3b3a28da5a2e43068583b683506e-libre.pdf?1697680298=\u0026response-content-disposition=attachment%3B+filename%3DThe_Effect_Of_Temperature_On_Recombinant.pdf\u0026Expires=1732596355\u0026Signature=Zb0-w41-IJQBs30fIFi0bipg2K3uFL8Cx8jKEEd3NipP-yF0cZot2EtLolT~DQNkzBIWiciEdENCH45WnaVgTVkReyduy28fooRWelhCX5vAJSDZvil6l8HKQ5Oowv1ezfIjYyNtcQgGwuabKm5iPUlitWUA1IXX~3aDKmqdIp6ie5DJQz39vSmS5v5kVusTmc1ZNGIGuOqoflW1~ro-Yvfa3cypNMqVos1~gElAlamACeLm30vceD8OpXfNFlZ-YR-E1bBJ~3lo0a6iby7xY5OQtchgvAWU06kczGVANyEMRSlOnyhnRWsh2j5w1PidI0d-9Ccufgnuvp7pzC0vrw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"The_Effect_Of_Temperature_On_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_Production_By_Pichia_pastoris_Expression_System","translated_slug":"","page_count":7,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737339,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737339/thumbnails/1.jpg","file_name":"e2d4189d3b3a28da5a2e43068583b683506e.pdf","download_url":"https://www.academia.edu/attachments/106737339/download_file?st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"The_Effect_Of_Temperature_On_Recombinant.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737339/e2d4189d3b3a28da5a2e43068583b683506e-libre.pdf?1697680298=\u0026response-content-disposition=attachment%3B+filename%3DThe_Effect_Of_Temperature_On_Recombinant.pdf\u0026Expires=1732596355\u0026Signature=Zb0-w41-IJQBs30fIFi0bipg2K3uFL8Cx8jKEEd3NipP-yF0cZot2EtLolT~DQNkzBIWiciEdENCH45WnaVgTVkReyduy28fooRWelhCX5vAJSDZvil6l8HKQ5Oowv1ezfIjYyNtcQgGwuabKm5iPUlitWUA1IXX~3aDKmqdIp6ie5DJQz39vSmS5v5kVusTmc1ZNGIGuOqoflW1~ro-Yvfa3cypNMqVos1~gElAlamACeLm30vceD8OpXfNFlZ-YR-E1bBJ~3lo0a6iby7xY5OQtchgvAWU06kczGVANyEMRSlOnyhnRWsh2j5w1PidI0d-9Ccufgnuvp7pzC0vrw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":151659,"name":"Yeast","url":"https://www.academia.edu/Documents/in/Yeast"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":283379,"name":"Glycerol","url":"https://www.academia.edu/Documents/in/Glycerol"}],"urls":[{"id":34836652,"url":"https://doi.org/10.14499/indonesianjpharm29iss2pp94"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322606"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322606/Comparison_of_Gene_Expression_Between_Two_Types_of_Anti_EGFRvIII_ScFv_Antibodies_Having_Different_Variable_Domain_Orders_in_and_lt_i_and_gt_Escherichia_coli_and_lt_i_and_gt"><img alt="Research paper thumbnail of Comparison of Gene Expression Between Two Types of Anti-EGFRvIII ScFv Antibodies Having Different Variable Domain Orders in &lt;i&gt;Escherichia coli&lt;/i&gt" class="work-thumbnail" src="https://attachments.academia-assets.com/106737338/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322606/Comparison_of_Gene_Expression_Between_Two_Types_of_Anti_EGFRvIII_ScFv_Antibodies_Having_Different_Variable_Domain_Orders_in_and_lt_i_and_gt_Escherichia_coli_and_lt_i_and_gt">Comparison of Gene Expression Between Two Types of Anti-EGFRvIII ScFv Antibodies Having Different Variable Domain Orders in &lt;i&gt;Escherichia coli&lt;/i&gt</a></div><div class="wp-workCard_item"><span>Annales Bogoriensis</span><span>, Jun 22, 2017</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="8ef89d6d891c104d85a247e4a6b9d2f2" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737338,"asset_id":108322606,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737338/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322606"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322606"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322606; 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To date, the effect of the order of variable domains in the expression of scFv antibodies against epidermal growth factor receptor variant III (EGFRvIII) has not been reported. This study aimed to compare the expression between VHlinker-VL and VL-linker-VH domain orders of the anti-EGFRvIII scFv antibodies in E. coli expression system. Recombinant plasmids inserted with DNA encoding scFv proteins were transformed into E. coli NiCo21 (DE3) competent cells and characterized by colony PCR. The expression of scFv proteins was done by using optimum concentration of inducer. Total proteins, soluble periplasmic and cytoplasmic proteins, also extracellular proteins were isolated, subsequently characterized by SDS-PAGE, Slot Blot, and ImageJ software analyses. The antigenbinding activity of both scFvs proteins against EGFRvIII was observed. The results showed that the relative percentage of scFv expression with VH-linker-VL domain order is higher than that of VL-linker-VH in each compartment. Moreover, both of scFvs proteins have antigen-binding activity against EGFRvIII.","publication_date":{"day":22,"month":6,"year":2017,"errors":{}},"publication_name":"Annales Bogoriensis","grobid_abstract_attachment_id":106737338},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322606/Comparison_of_Gene_Expression_Between_Two_Types_of_Anti_EGFRvIII_ScFv_Antibodies_Having_Different_Variable_Domain_Orders_in_and_lt_i_and_gt_Escherichia_coli_and_lt_i_and_gt","translated_internal_url":"","created_at":"2023-10-18T18:12:03.368-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737338,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737338/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737338/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Comparison_of_Gene_Expression_Between_Tw.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737338/pdf-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DComparison_of_Gene_Expression_Between_Tw.pdf\u0026Expires=1732596356\u0026Signature=bbZ1YeoDLfGuNwBTYRFOLVEUQW7BI6GGuy2UJ~1E~HETVizp1WP-LIpA7F~clDdgfd3bZXpXtQoIqCbAiVxb5nWSED5LIU0wlwJriZOkr06a4M2iHd8aF~CObvnibdCh7DBt7HFNZDWJO~~wBzuVDv~-qmLpTmiu50it3Z9PGPCFSx2ub7zLl5xRHvpIZMuGHNTODVXS0Lp-OrWpsNvAUEaAZ5mBRXgv7juYljH6VTlZDuuhBAhy4eNVOHnflvnyrqYU4Y2DN45uC1zQIbVaQUxUZNP9kpQOpCh8FioYJZfHXAKlLNZXb6mpDeUWKNu1vFDTjyvtK-HY81MWGrRr2Q__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Comparison_of_Gene_Expression_Between_Two_Types_of_Anti_EGFRvIII_ScFv_Antibodies_Having_Different_Variable_Domain_Orders_in_and_lt_i_and_gt_Escherichia_coli_and_lt_i_and_gt","translated_slug":"","page_count":9,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737338,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737338/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737338/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Comparison_of_Gene_Expression_Between_Tw.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737338/pdf-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DComparison_of_Gene_Expression_Between_Tw.pdf\u0026Expires=1732596356\u0026Signature=bbZ1YeoDLfGuNwBTYRFOLVEUQW7BI6GGuy2UJ~1E~HETVizp1WP-LIpA7F~clDdgfd3bZXpXtQoIqCbAiVxb5nWSED5LIU0wlwJriZOkr06a4M2iHd8aF~CObvnibdCh7DBt7HFNZDWJO~~wBzuVDv~-qmLpTmiu50it3Z9PGPCFSx2ub7zLl5xRHvpIZMuGHNTODVXS0Lp-OrWpsNvAUEaAZ5mBRXgv7juYljH6VTlZDuuhBAhy4eNVOHnflvnyrqYU4Y2DN45uC1zQIbVaQUxUZNP9kpQOpCh8FioYJZfHXAKlLNZXb6mpDeUWKNu1vFDTjyvtK-HY81MWGrRr2Q__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":1114508,"name":"Plasmid","url":"https://www.academia.edu/Documents/in/Plasmid"},{"id":1159037,"name":"Fusion Protein","url":"https://www.academia.edu/Documents/in/Fusion_Protein"},{"id":2095314,"name":"Linker","url":"https://www.academia.edu/Documents/in/Linker"}],"urls":[{"id":34836650,"url":"https://doi.org/10.14203/ann.bogor.2017.v21.n1.29-37"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322604"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322604/Improving_the_Expression_of_Human_Granulocyte_Colony_Stimulating_Factor_in_Escherichia_coli_by_Reducing_the_GC_content_and_Increasing_mRNA_Folding_Free_Energy_at_5_Terminal_End"><img alt="Research paper thumbnail of Improving the Expression of Human Granulocyte Colony Stimulating Factor in Escherichia coli by Reducing the GC-content and Increasing mRNA Folding Free Energy at 5’-Terminal End" class="work-thumbnail" src="https://attachments.academia-assets.com/106737336/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322604/Improving_the_Expression_of_Human_Granulocyte_Colony_Stimulating_Factor_in_Escherichia_coli_by_Reducing_the_GC_content_and_Increasing_mRNA_Folding_Free_Energy_at_5_Terminal_End">Improving the Expression of Human Granulocyte Colony Stimulating Factor in Escherichia coli by Reducing the GC-content and Increasing mRNA Folding Free Energy at 5’-Terminal End</a></div><div class="wp-workCard_item"><span>Advanced Pharmaceutical Bulletin</span><span>, Aug 9, 2020</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="d9ae5e68934183232c68c7911dc1bd6a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737336,"asset_id":108322604,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737336/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322604"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322604"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322604; 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dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "d9ae5e68934183232c68c7911dc1bd6a" } } $('.js-work-strip[data-work-id=108322604]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322604,"title":"Improving the Expression of Human Granulocyte Colony Stimulating Factor in Escherichia coli by Reducing the GC-content and Increasing mRNA Folding Free Energy at 5’-Terminal End","translated_title":"","metadata":{"publisher":"Tabriz University of Medical Sciences","grobid_abstract":"The cell cycle system is controlled in a timely manner by three groups of cyclins, cyclin dependent kinases and cyclin dependent kinase inhibitors. Abnormal alterations of cell cycle regulatory mechanisms are a common feature of many diseases including numerous tumor types such as ovarian cancer. Although a variety of cell cycle regulatory genes are well known in mammalian species including human and mice, they are not well studied in avian species, especially in laying hens which are recognized as an excellent animal model for research relevant to human ovarian carcinogenesis. Therefore, in the present study, we focused on comparative expression and regulation of expression of candidate genes which might be involved in the cell cycle program in surface epithelial ovarian cancer in laying hens. Our current results indicate that expression levels of cell cycle gene transcripts are greater in cancerous as compared to normal ovaries. In particular, cyclin A2 (CCNA2), CCND1, CCND2, CCND3, CCNE2, cyclin dependent kinase 1 (CDK1), CDK3, CDK5, cyclin dependent kinases inhibitor 1A (CDKN1A) and CDKN1B were upregulated predominantly in the glandular epithelia of cancerous ovaries from laying hens. Further, several microRNAs (miRs), specifically miR-1798, miR-1699, miR-223 and miR-1744 were discovered to influence expression of CCND1, CCNE2, CDK1, and CDK3 mRNAs, respectively, via their 39-UTR which suggests that posttranscriptional regulation of gene expression influences their expression in laying hens. Moreover, miR-1626 influenced CDKN1A expression and miR-222, miR-1787 and miR-1812 regulated CDKN1B expression via their 39-UTR regions. Collectively, results of the present study demonstrate increased expression of cell cycle-related genes in cancerous ovaries of laying hens and indicate that expression of these genes is post-transcriptionally regulated by specific microRNAs.","publication_date":{"day":9,"month":8,"year":2020,"errors":{}},"publication_name":"Advanced Pharmaceutical Bulletin","grobid_abstract_attachment_id":106737336},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322604/Improving_the_Expression_of_Human_Granulocyte_Colony_Stimulating_Factor_in_Escherichia_coli_by_Reducing_the_GC_content_and_Increasing_mRNA_Folding_Free_Energy_at_5_Terminal_End","translated_internal_url":"","created_at":"2023-10-18T18:12:03.081-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737336,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737336/thumbnails/1.jpg","file_name":"apb-10-610.pdf","download_url":"https://www.academia.edu/attachments/106737336/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Improving_the_Expression_of_Human_Granul.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737336/apb-10-610-libre.pdf?1697680298=\u0026response-content-disposition=attachment%3B+filename%3DImproving_the_Expression_of_Human_Granul.pdf\u0026Expires=1732596356\u0026Signature=BO8w2dwHf6fQMhHNSVDYe4BA43~tIF-JeNy1nN3~ubt46kRWLJ3kFKhgZNVCjYGKsfrlWTLbDFZOqQco3mZzzePt5KSg~9Ts5RCW14mvlCnFtAABX5BObfVb3~k1qAXq7J3zAoj~VT--z5cO13n1KaZIn5W2kq4qJdkdIy6oI891fpLpdw-ZqvU9bug1qP2nE8PaQr-ERsWp18TlxKGGjWXuaT61zfPEqRiuaiNjezGU6WuBpxibo0vYEcol9gq58pHf7ZdysVJds-7Jtg6VsNls2U9Ema1EVmuGw-U18V4soUEWhpxW-TY03J~AOWcva6sgJLINq43qnR8RrT1t6g__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Improving_the_Expression_of_Human_Granulocyte_Colony_Stimulating_Factor_in_Escherichia_coli_by_Reducing_the_GC_content_and_Increasing_mRNA_Folding_Free_Energy_at_5_Terminal_End","translated_slug":"","page_count":11,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737336,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737336/thumbnails/1.jpg","file_name":"apb-10-610.pdf","download_url":"https://www.academia.edu/attachments/106737336/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Improving_the_Expression_of_Human_Granul.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737336/apb-10-610-libre.pdf?1697680298=\u0026response-content-disposition=attachment%3B+filename%3DImproving_the_Expression_of_Human_Granul.pdf\u0026Expires=1732596356\u0026Signature=BO8w2dwHf6fQMhHNSVDYe4BA43~tIF-JeNy1nN3~ubt46kRWLJ3kFKhgZNVCjYGKsfrlWTLbDFZOqQco3mZzzePt5KSg~9Ts5RCW14mvlCnFtAABX5BObfVb3~k1qAXq7J3zAoj~VT--z5cO13n1KaZIn5W2kq4qJdkdIy6oI891fpLpdw-ZqvU9bug1qP2nE8PaQr-ERsWp18TlxKGGjWXuaT61zfPEqRiuaiNjezGU6WuBpxibo0vYEcol9gq58pHf7ZdysVJds-7Jtg6VsNls2U9Ema1EVmuGw-U18V4soUEWhpxW-TY03J~AOWcva6sgJLINq43qnR8RrT1t6g__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":129401,"name":"GC content","url":"https://www.academia.edu/Documents/in/GC_content"},{"id":844925,"name":"Open Reading Frame","url":"https://www.academia.edu/Documents/in/Open_Reading_Frame"},{"id":3989376,"name":"Codon usage bias","url":"https://www.academia.edu/Documents/in/Codon_usage_bias"}],"urls":[{"id":34836649,"url":"https://doi.org/10.34172/apb.2020.073"}]}, dispatcherData: dispatcherData }); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322600"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322600/Construction_of_Saccharomyces_cerevisiae_KEX2_650_gene_expression_vector_and_its_introduction_into_Escherichia_coli_DH5"><img alt="Research paper thumbnail of Construction of Saccharomyces cerevisiae KEX2-650 gene expression vector and its introduction into Escherichia coli DH5?" class="work-thumbnail" src="https://attachments.academia-assets.com/106737343/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322600/Construction_of_Saccharomyces_cerevisiae_KEX2_650_gene_expression_vector_and_its_introduction_into_Escherichia_coli_DH5">Construction of Saccharomyces cerevisiae KEX2-650 gene expression vector and its introduction into Escherichia coli DH5?</a></div><div class="wp-workCard_item"><span>Biodiversitas</span><span>, Aug 15, 2022</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="70430cdec9a9063ed43823a70b1d1500" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737343,"asset_id":108322600,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737343/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322600"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322600"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322600; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322600]").text(description); $(".js-view-count[data-work-id=108322600]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322600; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322600']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322600, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); 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Kex2 has a unique function, the conversion process of recombinant protein precursor into mature protein. Kex2 from Saccharomyces cerevisiae has similar functions also with furin in mammals (about 47% of sequence similarity). To gain advantage, extracellular Kex2 would be highly favorable for this process. This study aimed to construct recombinant Kex2 that could be produced extracellularly in Pichia pastoris host through pD902-KEX2-699 vector (synthetic) with FLAG-tag and 6 His-tag by removing most of C-terminal region, including transmembrane domain (TMD) from KEX2 gene sequence. Constructed KEX2 is the KEX2-650 variant with TMD and cytoplasmic domain deletion. The recombinant plasmid was constructed through site-directed mutagenesis using FP-Kex2-699 and RP-Kex2-650 primers, including the BamHI site for plasmid religation. PCR site-directed mutagenesis produces an amplicon DNA with an expected length of 5551 bp. After restriction (BamHI) and religation, the plasmid was reintroduced into Escherichia coli DH5α and obtained 16 colonies. Verification PCR target gene showed that clones number 9 produced an amplicon of the expected length (646 bp). DNA sequencing analysis confirmed that TMD was removed from the gene construct to form the KEX2-650 construct.","publication_date":{"day":15,"month":8,"year":2022,"errors":{}},"publication_name":"Biodiversitas","grobid_abstract_attachment_id":106737343},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322600/Construction_of_Saccharomyces_cerevisiae_KEX2_650_gene_expression_vector_and_its_introduction_into_Escherichia_coli_DH5","translated_internal_url":"","created_at":"2023-10-18T18:12:02.503-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737343,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737343/thumbnails/1.jpg","file_name":"6044.pdf","download_url":"https://www.academia.edu/attachments/106737343/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Construction_of_Saccharomyces_cerevisiae.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737343/6044-libre.pdf?1697680295=\u0026response-content-disposition=attachment%3B+filename%3DConstruction_of_Saccharomyces_cerevisiae.pdf\u0026Expires=1732596356\u0026Signature=Zm-hwfpLZefqw3LlRObfypXHtmKvzZ3phI7WOekspaeJeVyZEPQm1UIycZOtremxiJVlbXHmwKZ04sUYI0oyRD2l1zWCV7e~T5uhr83fOqaJaAno~6wdTIXuDe0NkTXM6Nf5CKMfYU5qmPzfCR5yAwec5ZUSpnsozYzRsBaZPHIyDNsGXXwuEqCnMcHq9Mj0b6KG2VayIbprVmWE6qK7S3ZFAad9vEDDU6tQ7S0ReZA-gL~~yfTJwcmOg~cQWj8uJ4cRSO3phlUB~Ih5vQvgARbs~zRqWLfaFz65SnFJVc~T~Y2NGT7Jqt8D42-Tk1Ju3nNq8Qnn8gOCmNU2shx9pQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Construction_of_Saccharomyces_cerevisiae_KEX2_650_gene_expression_vector_and_its_introduction_into_Escherichia_coli_DH5","translated_slug":"","page_count":8,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737343,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737343/thumbnails/1.jpg","file_name":"6044.pdf","download_url":"https://www.academia.edu/attachments/106737343/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Construction_of_Saccharomyces_cerevisiae.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737343/6044-libre.pdf?1697680295=\u0026response-content-disposition=attachment%3B+filename%3DConstruction_of_Saccharomyces_cerevisiae.pdf\u0026Expires=1732596356\u0026Signature=Zm-hwfpLZefqw3LlRObfypXHtmKvzZ3phI7WOekspaeJeVyZEPQm1UIycZOtremxiJVlbXHmwKZ04sUYI0oyRD2l1zWCV7e~T5uhr83fOqaJaAno~6wdTIXuDe0NkTXM6Nf5CKMfYU5qmPzfCR5yAwec5ZUSpnsozYzRsBaZPHIyDNsGXXwuEqCnMcHq9Mj0b6KG2VayIbprVmWE6qK7S3ZFAad9vEDDU6tQ7S0ReZA-gL~~yfTJwcmOg~cQWj8uJ4cRSO3phlUB~Ih5vQvgARbs~zRqWLfaFz65SnFJVc~T~Y2NGT7Jqt8D42-Tk1Ju3nNq8Qnn8gOCmNU2shx9pQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":49123,"name":"Saccharomyces cerevisiae","url":"https://www.academia.edu/Documents/in/Saccharomyces_cerevisiae"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":181936,"name":"Gene","url":"https://www.academia.edu/Documents/in/Gene"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":727072,"name":"Biodiversitas","url":"https://www.academia.edu/Documents/in/Biodiversitas"},{"id":1114508,"name":"Plasmid","url":"https://www.academia.edu/Documents/in/Plasmid"}],"urls":[{"id":34836644,"url":"https://doi.org/10.13057/biodiv/d230853"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322598"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322598/Desain_dan_Konstruksi_Gen_CSF3_Sintetik_CSF3syn_mengandung_kodon_preferensi_Escherichia_coli_dengan_teknik_PCR"><img alt="Research paper thumbnail of Desain dan Konstruksi Gen CSF3 Sintetik (CSF3syn) mengandung kodon preferensi Escherichia coli dengan teknik PCR" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322598/Desain_dan_Konstruksi_Gen_CSF3_Sintetik_CSF3syn_mengandung_kodon_preferensi_Escherichia_coli_dengan_teknik_PCR">Desain dan Konstruksi Gen CSF3 Sintetik (CSF3syn) mengandung kodon preferensi Escherichia coli dengan teknik PCR</a></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322598"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322598"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322598; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322594"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322594/Peningkatan_ekspresi_heterologus_dan_produksi_human_erythropoietin_rekombinan_pada_yeast_Pichia_pastoris_melalui_perubahan_kodon_usage_gen_hEPO"><img alt="Research paper thumbnail of Peningkatan ekspresi heterologus dan produksi human erythropoietin rekombinan pada yeast Pichia pastoris melalui perubahan kodon-usage gen hEPO" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322594/Peningkatan_ekspresi_heterologus_dan_produksi_human_erythropoietin_rekombinan_pada_yeast_Pichia_pastoris_melalui_perubahan_kodon_usage_gen_hEPO">Peningkatan ekspresi heterologus dan produksi human erythropoietin rekombinan pada yeast Pichia pastoris melalui perubahan kodon-usage gen hEPO</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Erythropoietin (EPO) adalah hormón yang mengatur proses erythropoiesis, yaitu proses pembentukan ...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Erythropoietin (EPO) adalah hormón yang mengatur proses erythropoiesis, yaitu proses pembentukan sel darah merah (erythrocytes) pada mamalia termasuk manusia. Humari-EPO merupakan glikoprotein, íerdiri atas 165 asam amino dan 4 sisi glikosilasi dengan ...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322594"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322594"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322594; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322594]").text(description); $(".js-view-count[data-work-id=108322594]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322594; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322594']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322594, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=108322594]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322594,"title":"Peningkatan ekspresi heterologus dan produksi human erythropoietin rekombinan pada yeast Pichia pastoris melalui perubahan kodon-usage gen hEPO","translated_title":"","metadata":{"abstract":"Erythropoietin (EPO) adalah hormón yang mengatur proses erythropoiesis, yaitu proses pembentukan sel darah merah (erythrocytes) pada mamalia termasuk manusia. Humari-EPO merupakan glikoprotein, íerdiri atas 165 asam amino dan 4 sisi glikosilasi dengan ...","publication_date":{"day":null,"month":null,"year":2007,"errors":{}}},"translated_abstract":"Erythropoietin (EPO) adalah hormón yang mengatur proses erythropoiesis, yaitu proses pembentukan sel darah merah (erythrocytes) pada mamalia termasuk manusia. Humari-EPO merupakan glikoprotein, íerdiri atas 165 asam amino dan 4 sisi glikosilasi dengan ...","internal_url":"https://www.academia.edu/108322594/Peningkatan_ekspresi_heterologus_dan_produksi_human_erythropoietin_rekombinan_pada_yeast_Pichia_pastoris_melalui_perubahan_kodon_usage_gen_hEPO","translated_internal_url":"","created_at":"2023-10-18T18:12:01.866-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Peningkatan_ekspresi_heterologus_dan_produksi_human_erythropoietin_rekombinan_pada_yeast_Pichia_pastoris_melalui_perubahan_kodon_usage_gen_hEPO","translated_slug":"","page_count":null,"language":"id","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[],"research_interests":[{"id":57802,"name":"Erythropoietin","url":"https://www.academia.edu/Documents/in/Erythropoietin"},{"id":151659,"name":"Yeast","url":"https://www.academia.edu/Documents/in/Yeast"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"}],"urls":[{"id":34836639,"url":"http://perpus.biotek.lipi.go.id/index.php?p=show_detail\u0026id=15218\u0026keywords="}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322593"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322593/Bioassay_of_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_rhG_CSF_for_Neutropenia_Treatment_in_Male_Sprague_Dawley_Rats"><img alt="Research paper thumbnail of Bioassay of Recombinant Human Granulocyte Colony Stimulating Factor (rhG-CSF) for Neutropenia Treatment in Male Sprague Dawley Rats" class="work-thumbnail" src="https://attachments.academia-assets.com/106737305/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322593/Bioassay_of_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_rhG_CSF_for_Neutropenia_Treatment_in_Male_Sprague_Dawley_Rats">Bioassay of Recombinant Human Granulocyte Colony Stimulating Factor (rhG-CSF) for Neutropenia Treatment in Male Sprague Dawley Rats</a></div><div class="wp-workCard_item"><span>MCBS (Molecular and Cellular Biomedical Sciences)</span><span>, Mar 1, 2020</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e221a94cd7a928ce3ad806bf0beea105" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737305,"asset_id":108322593,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737305/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322593"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322593"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322593; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322593]").text(description); $(".js-view-count[data-work-id=108322593]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322593; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322593']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322593, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "e221a94cd7a928ce3ad806bf0beea105" } } $('.js-work-strip[data-work-id=108322593]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322593,"title":"Bioassay of Recombinant Human Granulocyte Colony Stimulating Factor (rhG-CSF) for Neutropenia Treatment in Male Sprague Dawley Rats","translated_title":"","metadata":{"publisher":"Cell and BioPharmaceutical Institute","grobid_abstract":"Background: Recombinant human granulocyte colony stimulating factor (rhG-CSF) is a first line therapy for neutropenia. However, it is less affordable for most patients in developing and poor countries. Therefore, biosimilar products are developed to suppress the cost of treatment, namely with rhG-CSF. This study aimed to explore the establishment of an affordable rhG-CSF that has similar potential to induce neutrophils recovery as the positive control. Materials and Methods: The rhG-CSF was expressed as inclusion body in Escherichia coli NiCo21(DE3). The inclusion body was then solubilized, refolded, purified and characterized prior to be used in the bioactivity assay. Cyclophosphamideinduced male Sprague Dawley rats were used as animal model and administered with rhG-CSF. Blood sample was collected at several points of time, before and after rhG-CSF treatments. Complete blood count and peripheral blood smear were conducted to investigate the activity of the rhG-CSF on each blood cells type, particularly neutrophil. Results: Specific activity on neutrophil proliferation was shown after treatments with our rhG-CSF and positive control. Positive control dose 40 mg/kg BW was statistically similar with that of the rhG-CSF dose 80 and 120 mg/kg BW. However, in neutropenic condition, recovery of neutrophil counts could not be achieved within 4 days of treatments. Thus, a longer treatment is needed to observe the activity of the rhG-CSF as an antineutropenia agent. Conclusion: The rhG-CSF has been proven having specific activity on neutrophil proliferation. However, improvement in the rhG-CSF preparation is still needed and longer administration of the rhG-CSF has to be applied in the future study.","publication_date":{"day":1,"month":3,"year":2020,"errors":{}},"publication_name":"MCBS (Molecular and Cellular Biomedical Sciences)","grobid_abstract_attachment_id":106737305},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322593/Bioassay_of_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_rhG_CSF_for_Neutropenia_Treatment_in_Male_Sprague_Dawley_Rats","translated_internal_url":"","created_at":"2023-10-18T18:12:01.614-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737305,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737305/thumbnails/1.jpg","file_name":"45.pdf","download_url":"https://www.academia.edu/attachments/106737305/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Bioassay_of_Recombinant_Human_Granulocyt.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737305/45-libre.pdf?1697680313=\u0026response-content-disposition=attachment%3B+filename%3DBioassay_of_Recombinant_Human_Granulocyt.pdf\u0026Expires=1732596356\u0026Signature=ex6YfOsBixwaTGvBYcZFcCgDxFn6Rk2GhlOWNvDrpVWhZ~U7OTO5VW2ohi7hzNw6-js~LMR5485bMUhDUQnDqFoKGGI~qmID3CAr1~L-mFJkz2nJbBzEAWyV0hcrPv4X~YwHC0HwJTYqI-Laqu~Q8~jJvbrA-MdjPxb5s0KIGPEN1w5ONv32ddUsE1FjaCDCpV~Po~Y18ctBSaK23aDz1OQ8QMDl0DJbwnbFpHjit~wPv0N5FO5dsJxziNhAW2ILJ0SWuRfxLtoBOTXPBA6KLMPZq-6w8kRh3yT7L27A7iv37pKltFVxZ9fuHJdDOPvT9s1hYHWivLn28sTUUScSJQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Bioassay_of_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_rhG_CSF_for_Neutropenia_Treatment_in_Male_Sprague_Dawley_Rats","translated_slug":"","page_count":9,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737305,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737305/thumbnails/1.jpg","file_name":"45.pdf","download_url":"https://www.academia.edu/attachments/106737305/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Bioassay_of_Recombinant_Human_Granulocyt.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737305/45-libre.pdf?1697680313=\u0026response-content-disposition=attachment%3B+filename%3DBioassay_of_Recombinant_Human_Granulocyt.pdf\u0026Expires=1732596356\u0026Signature=ex6YfOsBixwaTGvBYcZFcCgDxFn6Rk2GhlOWNvDrpVWhZ~U7OTO5VW2ohi7hzNw6-js~LMR5485bMUhDUQnDqFoKGGI~qmID3CAr1~L-mFJkz2nJbBzEAWyV0hcrPv4X~YwHC0HwJTYqI-Laqu~Q8~jJvbrA-MdjPxb5s0KIGPEN1w5ONv32ddUsE1FjaCDCpV~Po~Y18ctBSaK23aDz1OQ8QMDl0DJbwnbFpHjit~wPv0N5FO5dsJxziNhAW2ILJ0SWuRfxLtoBOTXPBA6KLMPZq-6w8kRh3yT7L27A7iv37pKltFVxZ9fuHJdDOPvT9s1hYHWivLn28sTUUScSJQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"},{"id":106737306,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737306/thumbnails/1.jpg","file_name":"45.pdf","download_url":"https://www.academia.edu/attachments/106737306/download_file","bulk_download_file_name":"Bioassay_of_Recombinant_Human_Granulocyt.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737306/45-libre.pdf?1697680311=\u0026response-content-disposition=attachment%3B+filename%3DBioassay_of_Recombinant_Human_Granulocyt.pdf\u0026Expires=1732596356\u0026Signature=PoEZt3VZja~mMHyvgFtpGnU6I~-iIViTdyA88quwH5R2hn7BQ58mGNosQGQDaNhh198XraDbj0HlvxjboOKoWEW9r-ff-DlsDP~PEieeTk4VLcbGZn2RiDpXGgzkYKy-MQkBrxc9m2HBLt8y1UxrSl~Nd3UAnUWytdI~zuydsCBThmSpFwACe~-wOgQ1kE23UHcPiCJxf5FEV9~jJPHfDloAs3s~gqAvnVeyXQ~~fUKFuzTfvxtM0woLrUN4qeWOItV5ikj5b3I2rdKthyWMVd~iT~Q5GjX0qv1APyZCcgNpA7mpvecheIYLIEDN5JRcfFRJi6~E81pqQC5IC~prMQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":140,"name":"Pharmacology","url":"https://www.academia.edu/Documents/in/Pharmacology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":2969290,"name":"neutropenia","url":"https://www.academia.edu/Documents/in/neutropenia"},{"id":3360152,"name":"Absolute Neutrophil Count","url":"https://www.academia.edu/Documents/in/Absolute_Neutrophil_Count"}],"urls":[{"id":34836638,"url":"https://cellbiopharm.com/ojs/index.php/MCBS/article/download/81/45"}]}, dispatcherData: dispatcherData }); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322619"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322619/Expression_of_recombinant_human_granulocyte_colony_stimulating_factor_in_Escherichia_coli_using_various_induction_methods"><img alt="Research paper thumbnail of Expression of recombinant human granulocyte-colony stimulating factor in Escherichia coli using various induction methods" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322619/Expression_of_recombinant_human_granulocyte_colony_stimulating_factor_in_Escherichia_coli_using_various_induction_methods">Expression of recombinant human granulocyte-colony stimulating factor in Escherichia coli using various induction methods</a></div><div class="wp-workCard_item"><span>IOP conference series</span><span>, Feb 1, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Granulocyte-colony stimulating factor (G-CSF) is a glycoprotein that has several therapeutic appl...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Granulocyte-colony stimulating factor (G-CSF) is a glycoprotein that has several therapeutic applications. It consists of 174 amino acids and manufactured by recombinant DNA technology. Until now, the Escherichia coli expression system is still become the first choice for producing recombinant proteins. It is because of this organism is simple to culture in low-cost medium and easy to scale up. In the course to find the most efficient way to produce a high yield of recombinant human G-CSF, we compared several types of medium with different induction methods. In this experiment, recombinant E. coli NiCo21(DE3) harbouring gene encoding rh-GCSF proteins were cultured in various media including auto-induction, non-induction, and IPTG-induction. To determine the protein expression profile, culture sampling was done every 12 h (up to 60 h). Then, the optical density at ʎ 600 nm was measured using UV spectrophotometer and rh-GCSF protein expression were characterized using SDS-PAGE and western blot analyses. ImageJ software was used to calculate the amount of rh-GCSF protein yield using Bovine Serum Albumin (BSA) with known concentration as a standard. Result of this experiment concluded that simple auto-induction medium from Imperial College could produce good amount of rh-GCSF proteins (117 µg/mL) with relatively low production cost and short incubation time.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322619"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322619"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322619; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322619]").text(description); $(".js-view-count[data-work-id=108322619]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322619; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322619']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322619, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=108322619]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322619,"title":"Expression of recombinant human granulocyte-colony stimulating factor in Escherichia coli using various induction methods","translated_title":"","metadata":{"abstract":"Granulocyte-colony stimulating factor (G-CSF) is a glycoprotein that has several therapeutic applications. It consists of 174 amino acids and manufactured by recombinant DNA technology. Until now, the Escherichia coli expression system is still become the first choice for producing recombinant proteins. It is because of this organism is simple to culture in low-cost medium and easy to scale up. In the course to find the most efficient way to produce a high yield of recombinant human G-CSF, we compared several types of medium with different induction methods. In this experiment, recombinant E. coli NiCo21(DE3) harbouring gene encoding rh-GCSF proteins were cultured in various media including auto-induction, non-induction, and IPTG-induction. To determine the protein expression profile, culture sampling was done every 12 h (up to 60 h). Then, the optical density at ʎ 600 nm was measured using UV spectrophotometer and rh-GCSF protein expression were characterized using SDS-PAGE and western blot analyses. ImageJ software was used to calculate the amount of rh-GCSF protein yield using Bovine Serum Albumin (BSA) with known concentration as a standard. Result of this experiment concluded that simple auto-induction medium from Imperial College could produce good amount of rh-GCSF proteins (117 µg/mL) with relatively low production cost and short incubation time.","publisher":"IOP Publishing","publication_date":{"day":1,"month":2,"year":2020,"errors":{}},"publication_name":"IOP conference series"},"translated_abstract":"Granulocyte-colony stimulating factor (G-CSF) is a glycoprotein that has several therapeutic applications. It consists of 174 amino acids and manufactured by recombinant DNA technology. Until now, the Escherichia coli expression system is still become the first choice for producing recombinant proteins. It is because of this organism is simple to culture in low-cost medium and easy to scale up. In the course to find the most efficient way to produce a high yield of recombinant human G-CSF, we compared several types of medium with different induction methods. In this experiment, recombinant E. coli NiCo21(DE3) harbouring gene encoding rh-GCSF proteins were cultured in various media including auto-induction, non-induction, and IPTG-induction. To determine the protein expression profile, culture sampling was done every 12 h (up to 60 h). Then, the optical density at ʎ 600 nm was measured using UV spectrophotometer and rh-GCSF protein expression were characterized using SDS-PAGE and western blot analyses. ImageJ software was used to calculate the amount of rh-GCSF protein yield using Bovine Serum Albumin (BSA) with known concentration as a standard. Result of this experiment concluded that simple auto-induction medium from Imperial College could produce good amount of rh-GCSF proteins (117 µg/mL) with relatively low production cost and short incubation time.","internal_url":"https://www.academia.edu/108322619/Expression_of_recombinant_human_granulocyte_colony_stimulating_factor_in_Escherichia_coli_using_various_induction_methods","translated_internal_url":"","created_at":"2023-10-18T18:12:06.076-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Expression_of_recombinant_human_granulocyte_colony_stimulating_factor_in_Escherichia_coli_using_various_induction_methods","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":2639492,"name":"IOP conference series-MSE","url":"https://www.academia.edu/Documents/in/IOP_conference_series-MSE"}],"urls":[{"id":34836664,"url":"https://doi.org/10.1088/1755-1315/439/1/012042"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322618"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322618/Optimization_of_expression_JTAT_protein_with_emphasis_on_transformation_efficiency_and_IPTG_concentration"><img alt="Research paper thumbnail of Optimization of expression JTAT protein with emphasis on transformation efficiency and IPTG concentration" class="work-thumbnail" src="https://attachments.academia-assets.com/106737342/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322618/Optimization_of_expression_JTAT_protein_with_emphasis_on_transformation_efficiency_and_IPTG_concentration">Optimization of expression JTAT protein with emphasis on transformation efficiency and IPTG concentration</a></div><div class="wp-workCard_item"><span>Journal of Genetic Engineering and Biotechnology</span><span>, Dec 1, 2017</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="79e6fc996316153bcf4470e8c0b09b01" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737342,"asset_id":108322618,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737342/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NCw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322618"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322618"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322618; 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This research was aimed to optimize the expression of Jembrana TAT (JTAT) protein with preparing Escherichia coli (E. coli) in advance using adopted methods of M1 (MgCl 2 + CaCl 2) and M2 (CaCl 2 + Glycerol). The best transformation efficiency resulting from a better transformation method was used to subsequent expression of JTAT protein. A synthetic tat gene encoding protein JTAT was previously cloned into pBT-hisC. Concentration of 200; 400; 600 mM IPTG was induced to a small volume culture (200 ml; OD 600 = 4), incubated for 3 h. Pellets were harvested by centrifugation (4000 rpm; 4°C; 15 min). Buffer B (10 mM Immidazole) was added into pellets, lysed by freeze-thaw followed by sonication. Supernatant was collected by centrifugation (10,000 rpm; 4°C; 20 min) and purified using Ni-NTA Agarose resin, released by elution buffer (E) containing 400 mM Immidazole to collect purified protein twice (E1, E2). The protein was characterized by SDS-PAGE and Western Blot (WB), quantified (at k595 nm) with BSA standard method in prior. The result showed that transformation efficiency was better in M2 (2.53 Â 10 6) than M1 (3.10 Â 10 5). The JTAT protein was expressed at a right size of 11.8 kDa. Concentration of 200 mM IPTG produced a significantly better protein yield (1.500 ± 0.089 mg/ml; P \u003c 0.05) than 600 mM IPTG (0.896 ± 0.052 mg/ml) and not different to 400 mM IPTG (1.298 ± 0.080 mg/ml). This research indicated that transformation efficiency needs to be taken account in prior of optimization of the protein expression.","publication_date":{"day":1,"month":12,"year":2017,"errors":{}},"publication_name":"Journal of Genetic Engineering and Biotechnology","grobid_abstract_attachment_id":106737342},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322618/Optimization_of_expression_JTAT_protein_with_emphasis_on_transformation_efficiency_and_IPTG_concentration","translated_internal_url":"","created_at":"2023-10-18T18:12:05.825-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737342,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737342/thumbnails/1.jpg","file_name":"main.PMC6296586.pdf","download_url":"https://www.academia.edu/attachments/106737342/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Optimization_of_expression_JTAT_protein.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737342/main.PMC6296586-libre.pdf?1697680287=\u0026response-content-disposition=attachment%3B+filename%3DOptimization_of_expression_JTAT_protein.pdf\u0026Expires=1732596354\u0026Signature=R4wG98bg~iS-QrlfOpKjkr5hu~-2s25CQDvpr3fO~52PXlzWl1j2okqUm4SaLWb7eDx4vDSMpbfk~zVKCUQsAtQk0nSY7jDa3rRctmSpc2hpNNDaPWp7VwfAprsQksfb7Ae6~v-5VBlKoN6fIESgnWsOKNFPPIA1WYd9NCDWV-cyhkUTt2-CxKM6W89cMWs9Uyv0LOO7imk9GBEHpVgM1kzQOmQowQzMgNcBIxyCcG5AKi6Bx3s1nSPpTC0cVAvhcW-gMhiK3MIH2jtZu4rev8n~EqN3h0syQXdmkAeIQV8X57JaQguJHl5t6UbYwRaCwS42XkyaXCHIBtlvTSmo1w__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Optimization_of_expression_JTAT_protein_with_emphasis_on_transformation_efficiency_and_IPTG_concentration","translated_slug":"","page_count":5,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737342,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737342/thumbnails/1.jpg","file_name":"main.PMC6296586.pdf","download_url":"https://www.academia.edu/attachments/106737342/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Optimization_of_expression_JTAT_protein.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737342/main.PMC6296586-libre.pdf?1697680287=\u0026response-content-disposition=attachment%3B+filename%3DOptimization_of_expression_JTAT_protein.pdf\u0026Expires=1732596354\u0026Signature=R4wG98bg~iS-QrlfOpKjkr5hu~-2s25CQDvpr3fO~52PXlzWl1j2okqUm4SaLWb7eDx4vDSMpbfk~zVKCUQsAtQk0nSY7jDa3rRctmSpc2hpNNDaPWp7VwfAprsQksfb7Ae6~v-5VBlKoN6fIESgnWsOKNFPPIA1WYd9NCDWV-cyhkUTt2-CxKM6W89cMWs9Uyv0LOO7imk9GBEHpVgM1kzQOmQowQzMgNcBIxyCcG5AKi6Bx3s1nSPpTC0cVAvhcW-gMhiK3MIH2jtZu4rev8n~EqN3h0syQXdmkAeIQV8X57JaQguJHl5t6UbYwRaCwS42XkyaXCHIBtlvTSmo1w__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":414331,"name":"Centrifugation","url":"https://www.academia.edu/Documents/in/Centrifugation"},{"id":482809,"name":"DICTIONARY OF BIOTECHNOLOGY AND GENETIC ENGINEERING","url":"https://www.academia.edu/Documents/in/DICTIONARY_OF_BIOTECHNOLOGY_AND_GENETIC_ENGINEERING"},{"id":960199,"name":"Sonication","url":"https://www.academia.edu/Documents/in/Sonication"},{"id":1256745,"name":"Lysis","url":"https://www.academia.edu/Documents/in/Lysis"}],"urls":[{"id":34836663,"url":"https://doi.org/10.1016/j.jgeb.2017.06.009"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322617"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322617/The_Effect_of_Growth_Condition_on_a_Soluble_Expression_of_Anti_EGFRvIII_Single_chain_Antibody_in_i_Escherichia_coli_i_NiCo21_DE3_"><img alt="Research paper thumbnail of The Effect of Growth Condition on a Soluble Expression of Anti-EGFRvIII Single-chain Antibody in <i>Escherichia coli</i> NiCo21(DE3)" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322617/The_Effect_of_Growth_Condition_on_a_Soluble_Expression_of_Anti_EGFRvIII_Single_chain_Antibody_in_i_Escherichia_coli_i_NiCo21_DE3_">The Effect of Growth Condition on a Soluble Expression of Anti-EGFRvIII Single-chain Antibody in <i>Escherichia coli</i> NiCo21(DE3)</a></div><div class="wp-workCard_item"><span>한국 미생물 생명공학회지</span><span>, Jun 28, 2021</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322617"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322617"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322617; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322616"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322616/Overproduction_and_Purification_of_Soluble_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_in_i_Escherichia_coli_i_Using_Thioredoxin_as_Fusion"><img alt="Research paper thumbnail of Overproduction and Purification of Soluble Recombinant Human Granulocyte Colony Stimulating Factor in <i>Escherichia coli</i> Using Thioredoxin as Fusion" class="work-thumbnail" src="https://attachments.academia-assets.com/106737341/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322616/Overproduction_and_Purification_of_Soluble_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_in_i_Escherichia_coli_i_Using_Thioredoxin_as_Fusion">Overproduction and Purification of Soluble Recombinant Human Granulocyte Colony Stimulating Factor in <i>Escherichia coli</i> Using Thioredoxin as Fusion</a></div><div class="wp-workCard_item"><span>Annales Bogoriensis</span><span>, Jun 22, 2017</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="0045cf626cc5de9210ab690c84db4fcd" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737341,"asset_id":108322616,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737341/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322616"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322616"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322616; 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The open reading frame of G-CSF was synthetically constructed in previous work and was codon optimized for best expression in E. coli. In this research, the gene was fused to thioredoxin (Trx) at the N-terminal in pET32 vector. The purpose of this research was to optimize the overproduction and purification processes to obtain high yield recombinant protein in soluble form, and to characterize the Trx-G-CSF fusion protein. Overproduction was performed using IPTG induction method for 3 and 6 hours. The protein was purified by Ni-NTA affinity chromatography and separated using gradient concentration of imidazole. The purified protein was then characterized by SDS-PAGE and Western Blot analysis. Further, enterokinase was used to separate G-CSF from the fusion protein. The purified form of G-CSF was subsequently characterized using Western Blot and mass spectrometry using MALDI-TOF. The results showed that the fusion protein was successfully produced in soluble part as much as 48.25% were obtained after 3 hours of induction. The yield of fusion protein was 67.37% from total protein (229.65 mg protein/L culture). The Western Blot analysis showed the G-CSF band at around 18.6 kDa. Mass spectrometry with MALDI-TOF/ TOF revealed that 25.86% of amino acid residue was recognized as part of human G-CSF sequence.","publication_date":{"day":22,"month":6,"year":2017,"errors":{}},"publication_name":"Annales Bogoriensis","grobid_abstract_attachment_id":106737341},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322616/Overproduction_and_Purification_of_Soluble_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_in_i_Escherichia_coli_i_Using_Thioredoxin_as_Fusion","translated_internal_url":"","created_at":"2023-10-18T18:12:05.376-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737341,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737341/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737341/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Overproduction_and_Purification_of_Solub.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737341/pdf-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DOverproduction_and_Purification_of_Solub.pdf\u0026Expires=1732596355\u0026Signature=ZKpTwFMPAGrWrv-bnq-sk~xgZjsBiIuz8jEJoe95-WX~MbEqGBsx4ZgIxbr~QlOfC0kduDJTsAzE3fk0AQGBn0Yi5XutANsb4aXSAbUu9hotxLQd7wKKEs3gL~-sa30M6oHwx3weS0yQQAoIPTiWTjLsUG1GeM5SFLeLRxO5xYajZV5Ig1epLjDt6wskPLGfgjsR7TBE3CmJy1QEncaw1oeg7FFCAWdTOzKieTfjvkAB5uZoVYzpQlaGf063t0zfpN~u5hg97cm08rRK3zekHxhElkTeVJItyBjlW6BuqExbw3XRSE4y9cY7ZHivJGCtxZRDa0DFYZqKZ3l0V349rw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Overproduction_and_Purification_of_Soluble_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_in_i_Escherichia_coli_i_Using_Thioredoxin_as_Fusion","translated_slug":"","page_count":8,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737341,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737341/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737341/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Overproduction_and_Purification_of_Solub.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737341/pdf-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DOverproduction_and_Purification_of_Solub.pdf\u0026Expires=1732596355\u0026Signature=ZKpTwFMPAGrWrv-bnq-sk~xgZjsBiIuz8jEJoe95-WX~MbEqGBsx4ZgIxbr~QlOfC0kduDJTsAzE3fk0AQGBn0Yi5XutANsb4aXSAbUu9hotxLQd7wKKEs3gL~-sa30M6oHwx3weS0yQQAoIPTiWTjLsUG1GeM5SFLeLRxO5xYajZV5Ig1epLjDt6wskPLGfgjsR7TBE3CmJy1QEncaw1oeg7FFCAWdTOzKieTfjvkAB5uZoVYzpQlaGf063t0zfpN~u5hg97cm08rRK3zekHxhElkTeVJItyBjlW6BuqExbw3XRSE4y9cY7ZHivJGCtxZRDa0DFYZqKZ3l0V349rw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":1159037,"name":"Fusion Protein","url":"https://www.academia.edu/Documents/in/Fusion_Protein"}],"urls":[{"id":34836661,"url":"https://doi.org/10.14203/ann.bogor.2017.v21.n1.1-8"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322615"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322615/Construction_and_Periplasmic_Expression_of_the_Anti_EGFRvIII_ScFv_Antibody_Gene_in_Escherichia_coli"><img alt="Research paper thumbnail of Construction and Periplasmic Expression of the Anti-EGFRvIII ScFv Antibody Gene in Escherichia coli" class="work-thumbnail" src="https://attachments.academia-assets.com/106737316/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322615/Construction_and_Periplasmic_Expression_of_the_Anti_EGFRvIII_ScFv_Antibody_Gene_in_Escherichia_coli">Construction and Periplasmic Expression of the Anti-EGFRvIII ScFv Antibody Gene in Escherichia coli</a></div><div class="wp-workCard_item"><span>Scientia Pharmaceutica</span><span>, 2016</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="59188f4cbd095636559481e76121fba2" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737316,"asset_id":108322615,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737316/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322615"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322615"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322615; 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H.","grobid_abstract":"In the previous study, we constructed an expression vector carrying the anti-EGFRvIII scFv antibody gene with V H-linker-V L orientation. The proteins were successfully produced in the periplasmic space of Escherichia coli. In this study, we substituted the inserted DNA with V L-linker-V H orientation of the anti-EGFRvIII scFv gene and analyzed its expression in E. coli. The DNA fragment was amplified from its cloning vector (pTz-rscFv), subsequently cloned into a previous expression vector containing the pelB signal sequence and his-tag, and then transformed into E. coli TOP10. The recombinant plasmids were characterized by restriction, PCR, and DNA sequencing analyses. The new anti-EGFRvIII scFv antibody proteins have been successfully expressed in the periplasmic compartment of E. coli Nico21(DE3) using 0.1 mM final concentration of IPTG induction. Total proteins, soluble periplasmic and cytoplasmic proteins, solubilized inclusion bodies, and extracellular proteins were analyzed by SDS-PAGE and Western Blot analyses. The results showed that soluble scFv proteins were found in all fractions except from the cytoplasmic space.","publication_date":{"day":null,"month":null,"year":2016,"errors":{}},"publication_name":"Scientia Pharmaceutica","grobid_abstract_attachment_id":106737316},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322615/Construction_and_Periplasmic_Expression_of_the_Anti_EGFRvIII_ScFv_Antibody_Gene_in_Escherichia_coli","translated_internal_url":"","created_at":"2023-10-18T18:12:05.117-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737316,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737316/thumbnails/1.jpg","file_name":"scipharm-84-00141.pdf","download_url":"https://www.academia.edu/attachments/106737316/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Construction_and_Periplasmic_Expression.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737316/scipharm-84-00141-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DConstruction_and_Periplasmic_Expression.pdf\u0026Expires=1732596355\u0026Signature=DMQxy2KHWv1F9aJ4tLDyBxOwuOOOCUY5A3AT8KLVRd8TzGmZolJVPU1lUi-8~BQRtfPtGPsK3AbBl8Ic73aarO-ROQEq9ZddZ8HqmZ8YlsrykG8XpJmpqOTWyos35Oa2jaoupkeCb8v3R7O0XUKjII4yDIhmjPquVbv73euwvzPnX3ScGswKyfM81InOvhmWp2GV5T~Swxw2XpazQ5VhP8OrzmsuOtJyTr16AoogYbXWJcBp2qyIssQO8ICdEfMCqmyqWU5v5rY4w5uxQN0bNDI1sddWMg-PYH4RanILvtWqaAtQaDfZsHJm6jDJF7urRUcJtoSAKkI8Q9qGj8b-qQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Construction_and_Periplasmic_Expression_of_the_Anti_EGFRvIII_ScFv_Antibody_Gene_in_Escherichia_coli","translated_slug":"","page_count":12,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737316,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737316/thumbnails/1.jpg","file_name":"scipharm-84-00141.pdf","download_url":"https://www.academia.edu/attachments/106737316/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Construction_and_Periplasmic_Expression.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737316/scipharm-84-00141-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DConstruction_and_Periplasmic_Expression.pdf\u0026Expires=1732596355\u0026Signature=DMQxy2KHWv1F9aJ4tLDyBxOwuOOOCUY5A3AT8KLVRd8TzGmZolJVPU1lUi-8~BQRtfPtGPsK3AbBl8Ic73aarO-ROQEq9ZddZ8HqmZ8YlsrykG8XpJmpqOTWyos35Oa2jaoupkeCb8v3R7O0XUKjII4yDIhmjPquVbv73euwvzPnX3ScGswKyfM81InOvhmWp2GV5T~Swxw2XpazQ5VhP8OrzmsuOtJyTr16AoogYbXWJcBp2qyIssQO8ICdEfMCqmyqWU5v5rY4w5uxQN0bNDI1sddWMg-PYH4RanILvtWqaAtQaDfZsHJm6jDJF7urRUcJtoSAKkI8Q9qGj8b-qQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":1114508,"name":"Plasmid","url":"https://www.academia.edu/Documents/in/Plasmid"},{"id":1159037,"name":"Fusion Protein","url":"https://www.academia.edu/Documents/in/Fusion_Protein"},{"id":1417742,"name":"Expression Vector","url":"https://www.academia.edu/Documents/in/Expression_Vector"}],"urls":[{"id":34836660,"url":"https://www.mdpi.com/2218-0532/84/1/141/pdf?version=1473211467"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322614"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322614/Heterologous_expression_of_Trichoderma_reesei_exoglucanase_Cel6A_in_Pichia_pastoris_under_the_control_of_GAP_promoter"><img alt="Research paper thumbnail of Heterologous expression of Trichoderma reesei exoglucanase (Cel6A) in Pichia pastoris under the control of GAP promoter" class="work-thumbnail" src="https://attachments.academia-assets.com/106737344/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322614/Heterologous_expression_of_Trichoderma_reesei_exoglucanase_Cel6A_in_Pichia_pastoris_under_the_control_of_GAP_promoter">Heterologous expression of Trichoderma reesei exoglucanase (Cel6A) in Pichia pastoris under the control of GAP promoter</a></div><div class="wp-workCard_item"><span>Nucleation and Atmospheric Aerosols</span><span>, 2019</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e7279f73ee5a6648a331f718ea390f89" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737344,"asset_id":108322614,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737344/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322614"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322614"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322614; 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dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "e7279f73ee5a6648a331f718ea390f89" } } $('.js-work-strip[data-work-id=108322614]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322614,"title":"Heterologous expression of Trichoderma reesei exoglucanase (Cel6A) in Pichia pastoris under the control of GAP promoter","translated_title":"","metadata":{"publisher":"American Institute of Physics","grobid_abstract":"Cellulolytic microorganisms produce several cellulase enzymes which have different specificities and modes of action. At least three types of cellulase (endo, exo, and β-glucosidase) are involved in the degradation of cellulose. One of them, exo-β-1,4 glucanase or cellobiohydrolase, can release either glucose or cellobiose from ends of cellulose chains. In this study, we tried to express an exoglucanase (Cel6A) gene heterologically in Pichia pastoris. The Cel6A gene was derived from Trichoderma reesei cellobiohydrolase 2 (CBH2). It was synthetically prepared, and codon optimized for best expression in yeast P. pastoris. The gene was placed under the regulation of the GAP promoter. The recombinant plasmid, named pLIPI-TrCel6A, inserted with T. reesei Cel6A (TrCel6A) gene has been integrated into P. pastoris SMD1168H genome, and the recombinant enzyme has been successfully expressed by P. pastoris with a major product showing a molecular size of around 50 kDa.","publication_date":{"day":null,"month":null,"year":2019,"errors":{}},"publication_name":"Nucleation and Atmospheric Aerosols","grobid_abstract_attachment_id":106737344},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322614/Heterologous_expression_of_Trichoderma_reesei_exoglucanase_Cel6A_in_Pichia_pastoris_under_the_control_of_GAP_promoter","translated_internal_url":"","created_at":"2023-10-18T18:12:04.901-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737344,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737344/thumbnails/1.jpg","file_name":"1.pdf","download_url":"https://www.academia.edu/attachments/106737344/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Heterologous_expression_of_Trichoderma_r.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737344/1-libre.pdf?1697680303=\u0026response-content-disposition=attachment%3B+filename%3DHeterologous_expression_of_Trichoderma_r.pdf\u0026Expires=1732596355\u0026Signature=gNluRZh95sm~Oc3YF6SfmN3B5ZP53-anQCotuwYJw0sMWC91hZaH57a8qZW9GzubDNAApxGYKE4NlOxAlQ36vja3Mehklpl28MoLiNkTb2Sd9mjYgcJf7fXSRiTauggjwCD8-GlNM8Tf0cA6aql~ukz6tuBLptsIVG9tgLIqWXZVSRugSv6sNo~5Wy3dyscxgM40d3Bll5f0IIdQylS3Zh~ihvKVRLi96MPYm2PqxXo9p~XPlFMRJc7oaHj8OGms02nGXSIBc4pmHNBXyOmg2V~UBdorxSe76ejvBQTRrBJhIUuR4D408X5OaLNIXsdVE2gyG1f0Ji-wCY3t7jjUVQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Heterologous_expression_of_Trichoderma_reesei_exoglucanase_Cel6A_in_Pichia_pastoris_under_the_control_of_GAP_promoter","translated_slug":"","page_count":10,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737344,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737344/thumbnails/1.jpg","file_name":"1.pdf","download_url":"https://www.academia.edu/attachments/106737344/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Heterologous_expression_of_Trichoderma_r.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737344/1-libre.pdf?1697680303=\u0026response-content-disposition=attachment%3B+filename%3DHeterologous_expression_of_Trichoderma_r.pdf\u0026Expires=1732596355\u0026Signature=gNluRZh95sm~Oc3YF6SfmN3B5ZP53-anQCotuwYJw0sMWC91hZaH57a8qZW9GzubDNAApxGYKE4NlOxAlQ36vja3Mehklpl28MoLiNkTb2Sd9mjYgcJf7fXSRiTauggjwCD8-GlNM8Tf0cA6aql~ukz6tuBLptsIVG9tgLIqWXZVSRugSv6sNo~5Wy3dyscxgM40d3Bll5f0IIdQylS3Zh~ihvKVRLi96MPYm2PqxXo9p~XPlFMRJc7oaHj8OGms02nGXSIBc4pmHNBXyOmg2V~UBdorxSe76ejvBQTRrBJhIUuR4D408X5OaLNIXsdVE2gyG1f0Ji-wCY3t7jjUVQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":43685,"name":"Cellulase","url":"https://www.academia.edu/Documents/in/Cellulase"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"},{"id":1398164,"name":"Trichoderma Reesei","url":"https://www.academia.edu/Documents/in/Trichoderma_Reesei"},{"id":2356118,"name":"Cellobiose","url":"https://www.academia.edu/Documents/in/Cellobiose"}],"urls":[{"id":34836659,"url":"https://doi.org/10.1063/1.5125548"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322613"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322613/Expression_and_characterization_of_Trichoderma_reesei_endoglucanase_II_in_Pichia_pastoris_under_the_regulation_of_the_GAP_promoter"><img alt="Research paper thumbnail of Expression and characterization of Trichoderma reesei endoglucanase II in Pichia pastoris under the regulation of the GAP promoter" class="work-thumbnail" src="https://attachments.academia-assets.com/106737315/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322613/Expression_and_characterization_of_Trichoderma_reesei_endoglucanase_II_in_Pichia_pastoris_under_the_regulation_of_the_GAP_promoter">Expression and characterization of Trichoderma reesei endoglucanase II in Pichia pastoris under the regulation of the GAP promoter</a></div><div class="wp-workCard_item"><span>Indonesian Journal of Biotechnology</span><span>, Dec 2, 2020</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ccb82b8fe82c545e12756eb44e30e5ee" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737315,"asset_id":108322613,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737315/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322613"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322613"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322613; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322613]").text(description); $(".js-view-count[data-work-id=108322613]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322613; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322613']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322613, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "ccb82b8fe82c545e12756eb44e30e5ee" } } $('.js-work-strip[data-work-id=108322613]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322613,"title":"Expression and characterization of Trichoderma reesei endoglucanase II in Pichia pastoris under the regulation of the GAP promoter","translated_title":"","metadata":{"publisher":"Gadjah Mada University","grobid_abstract":"Trichoderma reesei is known to be one of the organisms capable for producing various types of cellulase in high concentrations. Among these cellulases, the highest catalytic efficiency of endoglucanases II (EGII, EC 3.2.1.4) are considered important for industrial application. The characterization of the EGII is necessary since it is widely used in high-temperature reactions in the industries. In this study, the recombinant EGII protein was expressed in Pichia pastoris and it has a molecular mass of approximately 52 kDa. Recombinant EGII was purified using Ni-NTA affinity chromatography and characterized by SDS-PAGE and western blot analyses. The enzyme activity of recombinant EGII was measured using the Nelson Somogyi method to determine its optimum pH and temperature. The result showed that the maximum EGII expression was achieved after 72 h of culture incubation. The crude enzyme has optimum activity at pH 5.0, resulting in 16.3 U/mL and 14.6 U/mL activity at 40°C and 50°C, respectively. While the purified enzyme gave the specific activity of 115.7 U/mg under the optimum condition. Finally, our study demonstrated that recombinant EGII could retain the endoglucanase activity for 89% and 80% at 40°C and 50°C, respectively.","publication_date":{"day":2,"month":12,"year":2020,"errors":{}},"publication_name":"Indonesian Journal of Biotechnology","grobid_abstract_attachment_id":106737315},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322613/Expression_and_characterization_of_Trichoderma_reesei_endoglucanase_II_in_Pichia_pastoris_under_the_regulation_of_the_GAP_promoter","translated_internal_url":"","created_at":"2023-10-18T18:12:04.667-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737315,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737315/thumbnails/1.jpg","file_name":"29994.pdf","download_url":"https://www.academia.edu/attachments/106737315/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Expression_and_characterization_of_Trich.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737315/29994-libre.pdf?1697680314=\u0026response-content-disposition=attachment%3B+filename%3DExpression_and_characterization_of_Trich.pdf\u0026Expires=1732596355\u0026Signature=eVatdK8A0UEsWQuNagMSVDQUmxf7vpXytks69GxRzxZA6svm5G7hGPBdIHykfhcE593~SzdpphWoUEwaCisaI4iMql82AnFo3az1oLQkDRctVJ0L0DJvMbuY6wpHfPp09Cl~cNDk5MUtbWL4J0P0uNdpzvqpiAG4Fuovzl6znqJ-jZQ5fQTen1q4N9WY9XD0RyZZG7nqTyyegxJe2W1yZFG0OmbMDaUBIWh~PCzrMoxzjqB2B62fsqRpiye0nfzQ1-sa4NLJfTz2z7Lfnmk54hincnp78lCx63YVzZ~szOYfea~k68UXAHhQAwx63K-n7n04NLPdRpG~uV8FWxa0sQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Expression_and_characterization_of_Trichoderma_reesei_endoglucanase_II_in_Pichia_pastoris_under_the_regulation_of_the_GAP_promoter","translated_slug":"","page_count":8,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737315,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737315/thumbnails/1.jpg","file_name":"29994.pdf","download_url":"https://www.academia.edu/attachments/106737315/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Expression_and_characterization_of_Trich.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737315/29994-libre.pdf?1697680314=\u0026response-content-disposition=attachment%3B+filename%3DExpression_and_characterization_of_Trich.pdf\u0026Expires=1732596355\u0026Signature=eVatdK8A0UEsWQuNagMSVDQUmxf7vpXytks69GxRzxZA6svm5G7hGPBdIHykfhcE593~SzdpphWoUEwaCisaI4iMql82AnFo3az1oLQkDRctVJ0L0DJvMbuY6wpHfPp09Cl~cNDk5MUtbWL4J0P0uNdpzvqpiAG4Fuovzl6znqJ-jZQ5fQTen1q4N9WY9XD0RyZZG7nqTyyegxJe2W1yZFG0OmbMDaUBIWh~PCzrMoxzjqB2B62fsqRpiye0nfzQ1-sa4NLJfTz2z7Lfnmk54hincnp78lCx63YVzZ~szOYfea~k68UXAHhQAwx63K-n7n04NLPdRpG~uV8FWxa0sQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":43685,"name":"Cellulase","url":"https://www.academia.edu/Documents/in/Cellulase"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"},{"id":201241,"name":"Affinity chromatography","url":"https://www.academia.edu/Documents/in/Affinity_chromatography"},{"id":231661,"name":"Enzyme","url":"https://www.academia.edu/Documents/in/Enzyme"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":420864,"name":"Universitas Gadjah Mada","url":"https://www.academia.edu/Documents/in/Universitas_Gadjah_Mada"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":585595,"name":"Molecular Mass","url":"https://www.academia.edu/Documents/in/Molecular_Mass"},{"id":954401,"name":"Enzyme Assay","url":"https://www.academia.edu/Documents/in/Enzyme_Assay"},{"id":1398164,"name":"Trichoderma Reesei","url":"https://www.academia.edu/Documents/in/Trichoderma_Reesei"}],"urls":[{"id":34836658,"url":"https://jurnal.ugm.ac.id/ijbiotech/article/download/55604/29994"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322612"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322612/Transformation_of_recombinant_plasmid_pJ404_EGFRvIII_bfp_into_an_Escherichia_coli_NiCo21_DE3_expression_host_and_its_characterization"><img alt="Research paper thumbnail of Transformation of recombinant plasmid pJ404-EGFRvIII-bfp into an Escherichia coli NiCo21(DE3) expression host and its characterization" class="work-thumbnail" src="https://attachments.academia-assets.com/106737340/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322612/Transformation_of_recombinant_plasmid_pJ404_EGFRvIII_bfp_into_an_Escherichia_coli_NiCo21_DE3_expression_host_and_its_characterization">Transformation of recombinant plasmid pJ404-EGFRvIII-bfp into an Escherichia coli NiCo21(DE3) expression host and its characterization</a></div><div class="wp-workCard_item"><span>IOP conference series</span><span>, Apr 28, 2020</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="45f6677e9115186d09a4c94578ca809e" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737340,"asset_id":108322612,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737340/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322612"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322612"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322612; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322612]").text(description); $(".js-view-count[data-work-id=108322612]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322612; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322612']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322612, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "45f6677e9115186d09a4c94578ca809e" } } $('.js-work-strip[data-work-id=108322612]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322612,"title":"Transformation of recombinant plasmid pJ404-EGFRvIII-bfp into an Escherichia coli NiCo21(DE3) expression host and its characterization","translated_title":"","metadata":{"publisher":"IOP Publishing","grobid_abstract":"Epidermal growth factor receptor variant III (EGFRvIII) is a mutant of epidermal growth factor receptor (EGFR) that lacks 267 amino acids (exons 2-7) within its extracellular domain that results in the formation of a new epitope as a tumor specific target. A synthetic gene of EGFRvIII has been constructed by previous researchers to encode a fusion protein as a marker in targeted cancer therapies. This research was conducted to transform the recombinant plasmid pJ404-EGFRvIII into Escherichia coli NiCo21(DE3) host cells and characterize the E. coli NiCo21(DE3) transformants. Recombinant plasmid pJ404-EGFRvIII was isolated with an alkali lysis method and transformed into E. coli NiCo21(DE3) by heat-shock method. The transformants were grown on LB medium containing100 Ɋg/ml ampicillin and characterized by colony PCR method. The results showed that the pJ404-EGFRvIII recombinant plasmid was transformed successfully into E. coli NiCo21(DE3). With the result that, EGFRvIII gene might be express by E. coli NiCo21(DE3) for further analysis of protein expression and purification in tumor terapy.","publication_date":{"day":28,"month":4,"year":2020,"errors":{}},"publication_name":"IOP conference series","grobid_abstract_attachment_id":106737340},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322612/Transformation_of_recombinant_plasmid_pJ404_EGFRvIII_bfp_into_an_Escherichia_coli_NiCo21_DE3_expression_host_and_its_characterization","translated_internal_url":"","created_at":"2023-10-18T18:12:04.420-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737340,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737340/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737340/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Transformation_of_recombinant_plasmid_pJ.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737340/pdf-libre.pdf?1697680290=\u0026response-content-disposition=attachment%3B+filename%3DTransformation_of_recombinant_plasmid_pJ.pdf\u0026Expires=1732596355\u0026Signature=IhBkWxIp82v11K6IK-oAIauYn~tgKR~01XhwfQW8ruYGg9NLmDSM8fjN5K2WSOH08B2nV6t8bvSskzQpYgi6p4QOH4tbB-yTJUG8Jj1KAURvDOU6w~~HPR8NfNICuhF09AHKuwqhtQs0rMhWamUc7iyHeKNwppm2b-xObEeD2YHYVCeQdoWwaGbnKaVZE~YKH2SvdyCzbUCMuxCr~iL4oulKkIwbxPKFdDef4K5Jin1qf1Pui656AkNHPQlbc1HLK8R3~geJ2-CoRZQKjOV4tV7h-vxYVzMl9XHPftGVg4on3gmWGPldI13C5tbjWWkR2Zw8wz5fzTWemWdz6ZateA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Transformation_of_recombinant_plasmid_pJ404_EGFRvIII_bfp_into_an_Escherichia_coli_NiCo21_DE3_expression_host_and_its_characterization","translated_slug":"","page_count":5,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737340,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737340/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737340/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Transformation_of_recombinant_plasmid_pJ.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737340/pdf-libre.pdf?1697680290=\u0026response-content-disposition=attachment%3B+filename%3DTransformation_of_recombinant_plasmid_pJ.pdf\u0026Expires=1732596355\u0026Signature=IhBkWxIp82v11K6IK-oAIauYn~tgKR~01XhwfQW8ruYGg9NLmDSM8fjN5K2WSOH08B2nV6t8bvSskzQpYgi6p4QOH4tbB-yTJUG8Jj1KAURvDOU6w~~HPR8NfNICuhF09AHKuwqhtQs0rMhWamUc7iyHeKNwppm2b-xObEeD2YHYVCeQdoWwaGbnKaVZE~YKH2SvdyCzbUCMuxCr~iL4oulKkIwbxPKFdDef4K5Jin1qf1Pui656AkNHPQlbc1HLK8R3~geJ2-CoRZQKjOV4tV7h-vxYVzMl9XHPftGVg4on3gmWGPldI13C5tbjWWkR2Zw8wz5fzTWemWdz6ZateA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":159,"name":"Microbiology","url":"https://www.academia.edu/Documents/in/Microbiology"},{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":1114508,"name":"Plasmid","url":"https://www.academia.edu/Documents/in/Plasmid"},{"id":2639492,"name":"IOP conference series-MSE","url":"https://www.academia.edu/Documents/in/IOP_conference_series-MSE"}],"urls":[{"id":34836657,"url":"https://doi.org/10.1088/1755-1315/481/1/012009"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322611"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322611/Purification_of_recombinant_human_granulocyte_colony_stimulating_factor_from_Pichia_pastoris_using_two_ninta_chromatography_methods"><img alt="Research paper thumbnail of Purification of recombinant human granulocyte colony-stimulating factor from Pichia pastoris using two ninta chromatography methods" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322611/Purification_of_recombinant_human_granulocyte_colony_stimulating_factor_from_Pichia_pastoris_using_two_ninta_chromatography_methods">Purification of recombinant human granulocyte colony-stimulating factor from Pichia pastoris using two ninta chromatography methods</a></div><div class="wp-workCard_item"><span>IOP conference series</span><span>, Feb 22, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Human granulocyte colony-stimulating factor (hG-CSF) is a glycoprotein that stimulates the produc...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Human granulocyte colony-stimulating factor (hG-CSF) is a glycoprotein that stimulates the production of mature neutrophil and enhances its survival, proliferation, differentiation, and neutrofil precursor function. This study was carried out to determine the purity of recombinant protein employing two purification methods using NiNTA with imidazole and with pH gradient (without imidazole). The synthetic gene (gcsf-cmyc) was cloned into secretive expression vector pPICZαA and methanol utilizing alcohol oxidase (AOX1) promoters before being expressed in Pichia pastoris SMD1168H strain. The recombinant protein was purified using NiNTA chromatography with imidazole and pH gradient. All samples were analyzed using SDS PAGE, followed with detection using coomasie blue. The molecular mass of recombinant hG-CSF expressed in P. pastoris was ∼23kD. The efficiency of hG-CSF purification using NiNTA with imidazole was ∼63%, while with pH gradient was ∼89%. Purification techniques use pH gradients gradients can be applied to avoid used of imidazole, so that it does not contaminate protein samples.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322611"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322611"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322611; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322611]").text(description); $(".js-view-count[data-work-id=108322611]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322611; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322611']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322611, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=108322611]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322611,"title":"Purification of recombinant human granulocyte colony-stimulating factor from Pichia pastoris using two ninta chromatography methods","translated_title":"","metadata":{"abstract":"Human granulocyte colony-stimulating factor (hG-CSF) is a glycoprotein that stimulates the production of mature neutrophil and enhances its survival, proliferation, differentiation, and neutrofil precursor function. This study was carried out to determine the purity of recombinant protein employing two purification methods using NiNTA with imidazole and with pH gradient (without imidazole). The synthetic gene (gcsf-cmyc) was cloned into secretive expression vector pPICZαA and methanol utilizing alcohol oxidase (AOX1) promoters before being expressed in Pichia pastoris SMD1168H strain. The recombinant protein was purified using NiNTA chromatography with imidazole and pH gradient. All samples were analyzed using SDS PAGE, followed with detection using coomasie blue. The molecular mass of recombinant hG-CSF expressed in P. pastoris was ∼23kD. The efficiency of hG-CSF purification using NiNTA with imidazole was ∼63%, while with pH gradient was ∼89%. Purification techniques use pH gradients gradients can be applied to avoid used of imidazole, so that it does not contaminate protein samples.","publisher":"IOP Publishing","publication_date":{"day":22,"month":2,"year":2020,"errors":{}},"publication_name":"IOP conference series"},"translated_abstract":"Human granulocyte colony-stimulating factor (hG-CSF) is a glycoprotein that stimulates the production of mature neutrophil and enhances its survival, proliferation, differentiation, and neutrofil precursor function. This study was carried out to determine the purity of recombinant protein employing two purification methods using NiNTA with imidazole and with pH gradient (without imidazole). The synthetic gene (gcsf-cmyc) was cloned into secretive expression vector pPICZαA and methanol utilizing alcohol oxidase (AOX1) promoters before being expressed in Pichia pastoris SMD1168H strain. The recombinant protein was purified using NiNTA chromatography with imidazole and pH gradient. All samples were analyzed using SDS PAGE, followed with detection using coomasie blue. The molecular mass of recombinant hG-CSF expressed in P. pastoris was ∼23kD. The efficiency of hG-CSF purification using NiNTA with imidazole was ∼63%, while with pH gradient was ∼89%. Purification techniques use pH gradients gradients can be applied to avoid used of imidazole, so that it does not contaminate protein samples.","internal_url":"https://www.academia.edu/108322611/Purification_of_recombinant_human_granulocyte_colony_stimulating_factor_from_Pichia_pastoris_using_two_ninta_chromatography_methods","translated_internal_url":"","created_at":"2023-10-18T18:12:04.126-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Purification_of_recombinant_human_granulocyte_colony_stimulating_factor_from_Pichia_pastoris_using_two_ninta_chromatography_methods","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":4656,"name":"Chromatography","url":"https://www.academia.edu/Documents/in/Chromatography"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":605726,"name":"Imidazole","url":"https://www.academia.edu/Documents/in/Imidazole"},{"id":2639492,"name":"IOP conference series-MSE","url":"https://www.academia.edu/Documents/in/IOP_conference_series-MSE"}],"urls":[{"id":34836656,"url":"https://doi.org/10.1088/1755-1315/439/1/012044"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322609"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322609/Bioinformatics_Analysis_to_Construct_Cellulose_binding_Module_Synthetic_Gene_and_Design_Primer"><img alt="Research paper thumbnail of Bioinformatics Analysis to Construct Cellulose-binding Module Synthetic Gene and Design Primer" class="work-thumbnail" src="https://attachments.academia-assets.com/106737337/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322609/Bioinformatics_Analysis_to_Construct_Cellulose_binding_Module_Synthetic_Gene_and_Design_Primer">Bioinformatics Analysis to Construct Cellulose-binding Module Synthetic Gene and Design Primer</a></div><div class="wp-workCard_item"><span>Bioedukasi (Jember)</span><span>, Jul 31, 2019</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="6edddf573ef964d55086f637cea0a848" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737337,"asset_id":108322609,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737337/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322609"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322609"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322609; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322609]").text(description); $(".js-view-count[data-work-id=108322609]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322609; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322609']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322609, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "6edddf573ef964d55086f637cea0a848" } } $('.js-work-strip[data-work-id=108322609]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322609,"title":"Bioinformatics Analysis to Construct Cellulose-binding Module Synthetic Gene and Design Primer","translated_title":"","metadata":{"publisher":"UPT Penerbitan Universitas Jember","grobid_abstract":"Cellulose-binding module (CBM) is a protein domain commonly found in various types of cellulase enzymes. The function of this CBM can be used for the binding process and the immobilization of a protein in the cellulose matrix. CBM can be obtained from several organisms, one of them is Trichoderma reesei. To get a gene, it does not have to be isolated from the original organism. Gene sequences can be obtained synthetically through bioinformatics analysis in accordance with the same gene sequences as those at Gene Bank. Bioinformatics analysis can be used to find new gene sequences or existing genes. This study aims to get a cbmsyn synthetic gene quickly and efficiently without reducing protein activity, which can then be ligated with other genes so that it functions as an immobilized enzyme. From the results of bioinformatics analysis, obtained DNA sequences measuring around 498 pb with 166 amino acid protein lengths. The sequence was modified by adding several restriction sites, namely BamHI, AfeI, and ScaI. 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322607"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322607/The_Effect_Of_Temperature_On_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_Production_By_Pichia_pastoris_Expression_System"><img alt="Research paper thumbnail of The Effect Of Temperature On Recombinant Human Granulocyte Colony Stimulating Factor Production By Pichia pastoris Expression System" class="work-thumbnail" src="https://attachments.academia-assets.com/106737339/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322607/The_Effect_Of_Temperature_On_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_Production_By_Pichia_pastoris_Expression_System">The Effect Of Temperature On Recombinant Human Granulocyte Colony Stimulating Factor Production By Pichia pastoris Expression System</a></div><div class="wp-workCard_item"><span>INDONESIAN JOURNAL OF PHARMACY</span><span>, Jul 10, 2018</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="9c6cfda2a0d94c4825104733d8888c8e" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737339,"asset_id":108322607,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737339/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322607"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322607"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322607; 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The main objective of this work is to compare the effect of different temperature on the production of extracellular recombinant G-CSF in Pichia pastoris. Cells were cultured for 72h in baffled shake-flasks at 20°C, 25°C, and 30°C in two different medium; buffered glycerol/methanol-complex medium (BMGY/BMMY) and buffered minimal glycerol/methanol (BMGH/BMMH) after methanol induction every 12h. Expressed recombinant hG-CSF in the methylotrophic yeast P. pastoris was analyzed with SDS-PAGE. The 23 kDa protein was secreted into the culture supernatant when induced with methanol. Production of recombinant G-CSF protein in P. pastoris at 30°C at 48h incubation after methanol induction every 12h is the highest in both complex and minimum medium.","publication_date":{"day":10,"month":7,"year":2018,"errors":{}},"publication_name":"INDONESIAN JOURNAL OF PHARMACY","grobid_abstract_attachment_id":106737339},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322607/The_Effect_Of_Temperature_On_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_Production_By_Pichia_pastoris_Expression_System","translated_internal_url":"","created_at":"2023-10-18T18:12:03.601-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737339,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737339/thumbnails/1.jpg","file_name":"e2d4189d3b3a28da5a2e43068583b683506e.pdf","download_url":"https://www.academia.edu/attachments/106737339/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"The_Effect_Of_Temperature_On_Recombinant.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737339/e2d4189d3b3a28da5a2e43068583b683506e-libre.pdf?1697680298=\u0026response-content-disposition=attachment%3B+filename%3DThe_Effect_Of_Temperature_On_Recombinant.pdf\u0026Expires=1732596355\u0026Signature=Zb0-w41-IJQBs30fIFi0bipg2K3uFL8Cx8jKEEd3NipP-yF0cZot2EtLolT~DQNkzBIWiciEdENCH45WnaVgTVkReyduy28fooRWelhCX5vAJSDZvil6l8HKQ5Oowv1ezfIjYyNtcQgGwuabKm5iPUlitWUA1IXX~3aDKmqdIp6ie5DJQz39vSmS5v5kVusTmc1ZNGIGuOqoflW1~ro-Yvfa3cypNMqVos1~gElAlamACeLm30vceD8OpXfNFlZ-YR-E1bBJ~3lo0a6iby7xY5OQtchgvAWU06kczGVANyEMRSlOnyhnRWsh2j5w1PidI0d-9Ccufgnuvp7pzC0vrw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"The_Effect_Of_Temperature_On_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_Production_By_Pichia_pastoris_Expression_System","translated_slug":"","page_count":7,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737339,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737339/thumbnails/1.jpg","file_name":"e2d4189d3b3a28da5a2e43068583b683506e.pdf","download_url":"https://www.academia.edu/attachments/106737339/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1NSw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"The_Effect_Of_Temperature_On_Recombinant.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737339/e2d4189d3b3a28da5a2e43068583b683506e-libre.pdf?1697680298=\u0026response-content-disposition=attachment%3B+filename%3DThe_Effect_Of_Temperature_On_Recombinant.pdf\u0026Expires=1732596355\u0026Signature=Zb0-w41-IJQBs30fIFi0bipg2K3uFL8Cx8jKEEd3NipP-yF0cZot2EtLolT~DQNkzBIWiciEdENCH45WnaVgTVkReyduy28fooRWelhCX5vAJSDZvil6l8HKQ5Oowv1ezfIjYyNtcQgGwuabKm5iPUlitWUA1IXX~3aDKmqdIp6ie5DJQz39vSmS5v5kVusTmc1ZNGIGuOqoflW1~ro-Yvfa3cypNMqVos1~gElAlamACeLm30vceD8OpXfNFlZ-YR-E1bBJ~3lo0a6iby7xY5OQtchgvAWU06kczGVANyEMRSlOnyhnRWsh2j5w1PidI0d-9Ccufgnuvp7pzC0vrw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":151659,"name":"Yeast","url":"https://www.academia.edu/Documents/in/Yeast"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":283379,"name":"Glycerol","url":"https://www.academia.edu/Documents/in/Glycerol"}],"urls":[{"id":34836652,"url":"https://doi.org/10.14499/indonesianjpharm29iss2pp94"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322606"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322606/Comparison_of_Gene_Expression_Between_Two_Types_of_Anti_EGFRvIII_ScFv_Antibodies_Having_Different_Variable_Domain_Orders_in_and_lt_i_and_gt_Escherichia_coli_and_lt_i_and_gt"><img alt="Research paper thumbnail of Comparison of Gene Expression Between Two Types of Anti-EGFRvIII ScFv Antibodies Having Different Variable Domain Orders in &lt;i&gt;Escherichia coli&lt;/i&gt" class="work-thumbnail" src="https://attachments.academia-assets.com/106737338/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322606/Comparison_of_Gene_Expression_Between_Two_Types_of_Anti_EGFRvIII_ScFv_Antibodies_Having_Different_Variable_Domain_Orders_in_and_lt_i_and_gt_Escherichia_coli_and_lt_i_and_gt">Comparison of Gene Expression Between Two Types of Anti-EGFRvIII ScFv Antibodies Having Different Variable Domain Orders in &lt;i&gt;Escherichia coli&lt;/i&gt</a></div><div class="wp-workCard_item"><span>Annales Bogoriensis</span><span>, Jun 22, 2017</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="8ef89d6d891c104d85a247e4a6b9d2f2" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737338,"asset_id":108322606,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737338/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322606"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322606"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322606; 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To date, the effect of the order of variable domains in the expression of scFv antibodies against epidermal growth factor receptor variant III (EGFRvIII) has not been reported. This study aimed to compare the expression between VHlinker-VL and VL-linker-VH domain orders of the anti-EGFRvIII scFv antibodies in E. coli expression system. Recombinant plasmids inserted with DNA encoding scFv proteins were transformed into E. coli NiCo21 (DE3) competent cells and characterized by colony PCR. The expression of scFv proteins was done by using optimum concentration of inducer. Total proteins, soluble periplasmic and cytoplasmic proteins, also extracellular proteins were isolated, subsequently characterized by SDS-PAGE, Slot Blot, and ImageJ software analyses. The antigenbinding activity of both scFvs proteins against EGFRvIII was observed. The results showed that the relative percentage of scFv expression with VH-linker-VL domain order is higher than that of VL-linker-VH in each compartment. Moreover, both of scFvs proteins have antigen-binding activity against EGFRvIII.","publication_date":{"day":22,"month":6,"year":2017,"errors":{}},"publication_name":"Annales Bogoriensis","grobid_abstract_attachment_id":106737338},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322606/Comparison_of_Gene_Expression_Between_Two_Types_of_Anti_EGFRvIII_ScFv_Antibodies_Having_Different_Variable_Domain_Orders_in_and_lt_i_and_gt_Escherichia_coli_and_lt_i_and_gt","translated_internal_url":"","created_at":"2023-10-18T18:12:03.368-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737338,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737338/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737338/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Comparison_of_Gene_Expression_Between_Tw.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737338/pdf-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DComparison_of_Gene_Expression_Between_Tw.pdf\u0026Expires=1732596356\u0026Signature=bbZ1YeoDLfGuNwBTYRFOLVEUQW7BI6GGuy2UJ~1E~HETVizp1WP-LIpA7F~clDdgfd3bZXpXtQoIqCbAiVxb5nWSED5LIU0wlwJriZOkr06a4M2iHd8aF~CObvnibdCh7DBt7HFNZDWJO~~wBzuVDv~-qmLpTmiu50it3Z9PGPCFSx2ub7zLl5xRHvpIZMuGHNTODVXS0Lp-OrWpsNvAUEaAZ5mBRXgv7juYljH6VTlZDuuhBAhy4eNVOHnflvnyrqYU4Y2DN45uC1zQIbVaQUxUZNP9kpQOpCh8FioYJZfHXAKlLNZXb6mpDeUWKNu1vFDTjyvtK-HY81MWGrRr2Q__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Comparison_of_Gene_Expression_Between_Two_Types_of_Anti_EGFRvIII_ScFv_Antibodies_Having_Different_Variable_Domain_Orders_in_and_lt_i_and_gt_Escherichia_coli_and_lt_i_and_gt","translated_slug":"","page_count":9,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737338,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737338/thumbnails/1.jpg","file_name":"pdf.pdf","download_url":"https://www.academia.edu/attachments/106737338/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Comparison_of_Gene_Expression_Between_Tw.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737338/pdf-libre.pdf?1697680296=\u0026response-content-disposition=attachment%3B+filename%3DComparison_of_Gene_Expression_Between_Tw.pdf\u0026Expires=1732596356\u0026Signature=bbZ1YeoDLfGuNwBTYRFOLVEUQW7BI6GGuy2UJ~1E~HETVizp1WP-LIpA7F~clDdgfd3bZXpXtQoIqCbAiVxb5nWSED5LIU0wlwJriZOkr06a4M2iHd8aF~CObvnibdCh7DBt7HFNZDWJO~~wBzuVDv~-qmLpTmiu50it3Z9PGPCFSx2ub7zLl5xRHvpIZMuGHNTODVXS0Lp-OrWpsNvAUEaAZ5mBRXgv7juYljH6VTlZDuuhBAhy4eNVOHnflvnyrqYU4Y2DN45uC1zQIbVaQUxUZNP9kpQOpCh8FioYJZfHXAKlLNZXb6mpDeUWKNu1vFDTjyvtK-HY81MWGrRr2Q__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":1114508,"name":"Plasmid","url":"https://www.academia.edu/Documents/in/Plasmid"},{"id":1159037,"name":"Fusion Protein","url":"https://www.academia.edu/Documents/in/Fusion_Protein"},{"id":2095314,"name":"Linker","url":"https://www.academia.edu/Documents/in/Linker"}],"urls":[{"id":34836650,"url":"https://doi.org/10.14203/ann.bogor.2017.v21.n1.29-37"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322604"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322604/Improving_the_Expression_of_Human_Granulocyte_Colony_Stimulating_Factor_in_Escherichia_coli_by_Reducing_the_GC_content_and_Increasing_mRNA_Folding_Free_Energy_at_5_Terminal_End"><img alt="Research paper thumbnail of Improving the Expression of Human Granulocyte Colony Stimulating Factor in Escherichia coli by Reducing the GC-content and Increasing mRNA Folding Free Energy at 5’-Terminal End" class="work-thumbnail" src="https://attachments.academia-assets.com/106737336/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322604/Improving_the_Expression_of_Human_Granulocyte_Colony_Stimulating_Factor_in_Escherichia_coli_by_Reducing_the_GC_content_and_Increasing_mRNA_Folding_Free_Energy_at_5_Terminal_End">Improving the Expression of Human Granulocyte Colony Stimulating Factor in Escherichia coli by Reducing the GC-content and Increasing mRNA Folding Free Energy at 5’-Terminal End</a></div><div class="wp-workCard_item"><span>Advanced Pharmaceutical Bulletin</span><span>, Aug 9, 2020</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="d9ae5e68934183232c68c7911dc1bd6a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737336,"asset_id":108322604,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737336/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322604"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322604"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322604; 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Abnormal alterations of cell cycle regulatory mechanisms are a common feature of many diseases including numerous tumor types such as ovarian cancer. Although a variety of cell cycle regulatory genes are well known in mammalian species including human and mice, they are not well studied in avian species, especially in laying hens which are recognized as an excellent animal model for research relevant to human ovarian carcinogenesis. Therefore, in the present study, we focused on comparative expression and regulation of expression of candidate genes which might be involved in the cell cycle program in surface epithelial ovarian cancer in laying hens. Our current results indicate that expression levels of cell cycle gene transcripts are greater in cancerous as compared to normal ovaries. In particular, cyclin A2 (CCNA2), CCND1, CCND2, CCND3, CCNE2, cyclin dependent kinase 1 (CDK1), CDK3, CDK5, cyclin dependent kinases inhibitor 1A (CDKN1A) and CDKN1B were upregulated predominantly in the glandular epithelia of cancerous ovaries from laying hens. Further, several microRNAs (miRs), specifically miR-1798, miR-1699, miR-223 and miR-1744 were discovered to influence expression of CCND1, CCNE2, CDK1, and CDK3 mRNAs, respectively, via their 39-UTR which suggests that posttranscriptional regulation of gene expression influences their expression in laying hens. Moreover, miR-1626 influenced CDKN1A expression and miR-222, miR-1787 and miR-1812 regulated CDKN1B expression via their 39-UTR regions. Collectively, results of the present study demonstrate increased expression of cell cycle-related genes in cancerous ovaries of laying hens and indicate that expression of these genes is post-transcriptionally regulated by specific microRNAs.","publication_date":{"day":9,"month":8,"year":2020,"errors":{}},"publication_name":"Advanced Pharmaceutical Bulletin","grobid_abstract_attachment_id":106737336},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322604/Improving_the_Expression_of_Human_Granulocyte_Colony_Stimulating_Factor_in_Escherichia_coli_by_Reducing_the_GC_content_and_Increasing_mRNA_Folding_Free_Energy_at_5_Terminal_End","translated_internal_url":"","created_at":"2023-10-18T18:12:03.081-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737336,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737336/thumbnails/1.jpg","file_name":"apb-10-610.pdf","download_url":"https://www.academia.edu/attachments/106737336/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Improving_the_Expression_of_Human_Granul.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737336/apb-10-610-libre.pdf?1697680298=\u0026response-content-disposition=attachment%3B+filename%3DImproving_the_Expression_of_Human_Granul.pdf\u0026Expires=1732596356\u0026Signature=BO8w2dwHf6fQMhHNSVDYe4BA43~tIF-JeNy1nN3~ubt46kRWLJ3kFKhgZNVCjYGKsfrlWTLbDFZOqQco3mZzzePt5KSg~9Ts5RCW14mvlCnFtAABX5BObfVb3~k1qAXq7J3zAoj~VT--z5cO13n1KaZIn5W2kq4qJdkdIy6oI891fpLpdw-ZqvU9bug1qP2nE8PaQr-ERsWp18TlxKGGjWXuaT61zfPEqRiuaiNjezGU6WuBpxibo0vYEcol9gq58pHf7ZdysVJds-7Jtg6VsNls2U9Ema1EVmuGw-U18V4soUEWhpxW-TY03J~AOWcva6sgJLINq43qnR8RrT1t6g__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Improving_the_Expression_of_Human_Granulocyte_Colony_Stimulating_Factor_in_Escherichia_coli_by_Reducing_the_GC_content_and_Increasing_mRNA_Folding_Free_Energy_at_5_Terminal_End","translated_slug":"","page_count":11,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737336,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737336/thumbnails/1.jpg","file_name":"apb-10-610.pdf","download_url":"https://www.academia.edu/attachments/106737336/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Improving_the_Expression_of_Human_Granul.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737336/apb-10-610-libre.pdf?1697680298=\u0026response-content-disposition=attachment%3B+filename%3DImproving_the_Expression_of_Human_Granul.pdf\u0026Expires=1732596356\u0026Signature=BO8w2dwHf6fQMhHNSVDYe4BA43~tIF-JeNy1nN3~ubt46kRWLJ3kFKhgZNVCjYGKsfrlWTLbDFZOqQco3mZzzePt5KSg~9Ts5RCW14mvlCnFtAABX5BObfVb3~k1qAXq7J3zAoj~VT--z5cO13n1KaZIn5W2kq4qJdkdIy6oI891fpLpdw-ZqvU9bug1qP2nE8PaQr-ERsWp18TlxKGGjWXuaT61zfPEqRiuaiNjezGU6WuBpxibo0vYEcol9gq58pHf7ZdysVJds-7Jtg6VsNls2U9Ema1EVmuGw-U18V4soUEWhpxW-TY03J~AOWcva6sgJLINq43qnR8RrT1t6g__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":129401,"name":"GC content","url":"https://www.academia.edu/Documents/in/GC_content"},{"id":844925,"name":"Open Reading Frame","url":"https://www.academia.edu/Documents/in/Open_Reading_Frame"},{"id":3989376,"name":"Codon usage bias","url":"https://www.academia.edu/Documents/in/Codon_usage_bias"}],"urls":[{"id":34836649,"url":"https://doi.org/10.34172/apb.2020.073"}]}, dispatcherData: dispatcherData }); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322600"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322600/Construction_of_Saccharomyces_cerevisiae_KEX2_650_gene_expression_vector_and_its_introduction_into_Escherichia_coli_DH5"><img alt="Research paper thumbnail of Construction of Saccharomyces cerevisiae KEX2-650 gene expression vector and its introduction into Escherichia coli DH5?" class="work-thumbnail" src="https://attachments.academia-assets.com/106737343/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322600/Construction_of_Saccharomyces_cerevisiae_KEX2_650_gene_expression_vector_and_its_introduction_into_Escherichia_coli_DH5">Construction of Saccharomyces cerevisiae KEX2-650 gene expression vector and its introduction into Escherichia coli DH5?</a></div><div class="wp-workCard_item"><span>Biodiversitas</span><span>, Aug 15, 2022</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="70430cdec9a9063ed43823a70b1d1500" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737343,"asset_id":108322600,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737343/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322600"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322600"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322600; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322600]").text(description); $(".js-view-count[data-work-id=108322600]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322600; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322600']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322600, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); 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Kex2 has a unique function, the conversion process of recombinant protein precursor into mature protein. Kex2 from Saccharomyces cerevisiae has similar functions also with furin in mammals (about 47% of sequence similarity). To gain advantage, extracellular Kex2 would be highly favorable for this process. This study aimed to construct recombinant Kex2 that could be produced extracellularly in Pichia pastoris host through pD902-KEX2-699 vector (synthetic) with FLAG-tag and 6 His-tag by removing most of C-terminal region, including transmembrane domain (TMD) from KEX2 gene sequence. Constructed KEX2 is the KEX2-650 variant with TMD and cytoplasmic domain deletion. The recombinant plasmid was constructed through site-directed mutagenesis using FP-Kex2-699 and RP-Kex2-650 primers, including the BamHI site for plasmid religation. PCR site-directed mutagenesis produces an amplicon DNA with an expected length of 5551 bp. After restriction (BamHI) and religation, the plasmid was reintroduced into Escherichia coli DH5α and obtained 16 colonies. Verification PCR target gene showed that clones number 9 produced an amplicon of the expected length (646 bp). DNA sequencing analysis confirmed that TMD was removed from the gene construct to form the KEX2-650 construct.","publication_date":{"day":15,"month":8,"year":2022,"errors":{}},"publication_name":"Biodiversitas","grobid_abstract_attachment_id":106737343},"translated_abstract":null,"internal_url":"https://www.academia.edu/108322600/Construction_of_Saccharomyces_cerevisiae_KEX2_650_gene_expression_vector_and_its_introduction_into_Escherichia_coli_DH5","translated_internal_url":"","created_at":"2023-10-18T18:12:02.503-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":106737343,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737343/thumbnails/1.jpg","file_name":"6044.pdf","download_url":"https://www.academia.edu/attachments/106737343/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Construction_of_Saccharomyces_cerevisiae.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737343/6044-libre.pdf?1697680295=\u0026response-content-disposition=attachment%3B+filename%3DConstruction_of_Saccharomyces_cerevisiae.pdf\u0026Expires=1732596356\u0026Signature=Zm-hwfpLZefqw3LlRObfypXHtmKvzZ3phI7WOekspaeJeVyZEPQm1UIycZOtremxiJVlbXHmwKZ04sUYI0oyRD2l1zWCV7e~T5uhr83fOqaJaAno~6wdTIXuDe0NkTXM6Nf5CKMfYU5qmPzfCR5yAwec5ZUSpnsozYzRsBaZPHIyDNsGXXwuEqCnMcHq9Mj0b6KG2VayIbprVmWE6qK7S3ZFAad9vEDDU6tQ7S0ReZA-gL~~yfTJwcmOg~cQWj8uJ4cRSO3phlUB~Ih5vQvgARbs~zRqWLfaFz65SnFJVc~T~Y2NGT7Jqt8D42-Tk1Ju3nNq8Qnn8gOCmNU2shx9pQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Construction_of_Saccharomyces_cerevisiae_KEX2_650_gene_expression_vector_and_its_introduction_into_Escherichia_coli_DH5","translated_slug":"","page_count":8,"language":"en","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[{"id":106737343,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/106737343/thumbnails/1.jpg","file_name":"6044.pdf","download_url":"https://www.academia.edu/attachments/106737343/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Construction_of_Saccharomyces_cerevisiae.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/106737343/6044-libre.pdf?1697680295=\u0026response-content-disposition=attachment%3B+filename%3DConstruction_of_Saccharomyces_cerevisiae.pdf\u0026Expires=1732596356\u0026Signature=Zm-hwfpLZefqw3LlRObfypXHtmKvzZ3phI7WOekspaeJeVyZEPQm1UIycZOtremxiJVlbXHmwKZ04sUYI0oyRD2l1zWCV7e~T5uhr83fOqaJaAno~6wdTIXuDe0NkTXM6Nf5CKMfYU5qmPzfCR5yAwec5ZUSpnsozYzRsBaZPHIyDNsGXXwuEqCnMcHq9Mj0b6KG2VayIbprVmWE6qK7S3ZFAad9vEDDU6tQ7S0ReZA-gL~~yfTJwcmOg~cQWj8uJ4cRSO3phlUB~Ih5vQvgARbs~zRqWLfaFz65SnFJVc~T~Y2NGT7Jqt8D42-Tk1Ju3nNq8Qnn8gOCmNU2shx9pQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":49123,"name":"Saccharomyces cerevisiae","url":"https://www.academia.edu/Documents/in/Saccharomyces_cerevisiae"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":181936,"name":"Gene","url":"https://www.academia.edu/Documents/in/Gene"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":727072,"name":"Biodiversitas","url":"https://www.academia.edu/Documents/in/Biodiversitas"},{"id":1114508,"name":"Plasmid","url":"https://www.academia.edu/Documents/in/Plasmid"}],"urls":[{"id":34836644,"url":"https://doi.org/10.13057/biodiv/d230853"}]}, dispatcherData: dispatcherData }); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322594"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322594/Peningkatan_ekspresi_heterologus_dan_produksi_human_erythropoietin_rekombinan_pada_yeast_Pichia_pastoris_melalui_perubahan_kodon_usage_gen_hEPO"><img alt="Research paper thumbnail of Peningkatan ekspresi heterologus dan produksi human erythropoietin rekombinan pada yeast Pichia pastoris melalui perubahan kodon-usage gen hEPO" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322594/Peningkatan_ekspresi_heterologus_dan_produksi_human_erythropoietin_rekombinan_pada_yeast_Pichia_pastoris_melalui_perubahan_kodon_usage_gen_hEPO">Peningkatan ekspresi heterologus dan produksi human erythropoietin rekombinan pada yeast Pichia pastoris melalui perubahan kodon-usage gen hEPO</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Erythropoietin (EPO) adalah hormón yang mengatur proses erythropoiesis, yaitu proses pembentukan ...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Erythropoietin (EPO) adalah hormón yang mengatur proses erythropoiesis, yaitu proses pembentukan sel darah merah (erythrocytes) pada mamalia termasuk manusia. Humari-EPO merupakan glikoprotein, íerdiri atas 165 asam amino dan 4 sisi glikosilasi dengan ...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322594"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322594"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322594; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=108322594]").text(description); $(".js-view-count[data-work-id=108322594]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 108322594; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='108322594']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 108322594, container: "", }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=108322594]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322594,"title":"Peningkatan ekspresi heterologus dan produksi human erythropoietin rekombinan pada yeast Pichia pastoris melalui perubahan kodon-usage gen hEPO","translated_title":"","metadata":{"abstract":"Erythropoietin (EPO) adalah hormón yang mengatur proses erythropoiesis, yaitu proses pembentukan sel darah merah (erythrocytes) pada mamalia termasuk manusia. Humari-EPO merupakan glikoprotein, íerdiri atas 165 asam amino dan 4 sisi glikosilasi dengan ...","publication_date":{"day":null,"month":null,"year":2007,"errors":{}}},"translated_abstract":"Erythropoietin (EPO) adalah hormón yang mengatur proses erythropoiesis, yaitu proses pembentukan sel darah merah (erythrocytes) pada mamalia termasuk manusia. Humari-EPO merupakan glikoprotein, íerdiri atas 165 asam amino dan 4 sisi glikosilasi dengan ...","internal_url":"https://www.academia.edu/108322594/Peningkatan_ekspresi_heterologus_dan_produksi_human_erythropoietin_rekombinan_pada_yeast_Pichia_pastoris_melalui_perubahan_kodon_usage_gen_hEPO","translated_internal_url":"","created_at":"2023-10-18T18:12:01.866-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":5187356,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Peningkatan_ekspresi_heterologus_dan_produksi_human_erythropoietin_rekombinan_pada_yeast_Pichia_pastoris_melalui_perubahan_kodon_usage_gen_hEPO","translated_slug":"","page_count":null,"language":"id","content_type":"Work","owner":{"id":5187356,"first_name":"Asrul","middle_initials":null,"last_name":"Fuad","page_name":"AsrulFuad","domain_name":"independent","created_at":"2013-08-19T14:21:18.741-07:00","display_name":"Asrul Fuad","url":"https://independent.academia.edu/AsrulFuad"},"attachments":[],"research_interests":[{"id":57802,"name":"Erythropoietin","url":"https://www.academia.edu/Documents/in/Erythropoietin"},{"id":151659,"name":"Yeast","url":"https://www.academia.edu/Documents/in/Yeast"},{"id":186037,"name":"Pichia pastoris","url":"https://www.academia.edu/Documents/in/Pichia_pastoris"}],"urls":[{"id":34836639,"url":"http://perpus.biotek.lipi.go.id/index.php?p=show_detail\u0026id=15218\u0026keywords="}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="108322593"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/108322593/Bioassay_of_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_rhG_CSF_for_Neutropenia_Treatment_in_Male_Sprague_Dawley_Rats"><img alt="Research paper thumbnail of Bioassay of Recombinant Human Granulocyte Colony Stimulating Factor (rhG-CSF) for Neutropenia Treatment in Male Sprague Dawley Rats" class="work-thumbnail" src="https://attachments.academia-assets.com/106737305/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/108322593/Bioassay_of_Recombinant_Human_Granulocyte_Colony_Stimulating_Factor_rhG_CSF_for_Neutropenia_Treatment_in_Male_Sprague_Dawley_Rats">Bioassay of Recombinant Human Granulocyte Colony Stimulating Factor (rhG-CSF) for Neutropenia Treatment in Male Sprague Dawley Rats</a></div><div class="wp-workCard_item"><span>MCBS (Molecular and Cellular Biomedical Sciences)</span><span>, Mar 1, 2020</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e221a94cd7a928ce3ad806bf0beea105" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":106737305,"asset_id":108322593,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/106737305/download_file?st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&st=MTczMjU5Mjc1Niw4LjIyMi4yMDguMTQ2&s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="108322593"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="108322593"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 108322593; 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dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "e221a94cd7a928ce3ad806bf0beea105" } } $('.js-work-strip[data-work-id=108322593]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":108322593,"title":"Bioassay of Recombinant Human Granulocyte Colony Stimulating Factor (rhG-CSF) for Neutropenia Treatment in Male Sprague Dawley Rats","translated_title":"","metadata":{"publisher":"Cell and BioPharmaceutical Institute","grobid_abstract":"Background: Recombinant human granulocyte colony stimulating factor (rhG-CSF) is a first line therapy for neutropenia. However, it is less affordable for most patients in developing and poor countries. Therefore, biosimilar products are developed to suppress the cost of treatment, namely with rhG-CSF. This study aimed to explore the establishment of an affordable rhG-CSF that has similar potential to induce neutrophils recovery as the positive control. Materials and Methods: The rhG-CSF was expressed as inclusion body in Escherichia coli NiCo21(DE3). The inclusion body was then solubilized, refolded, purified and characterized prior to be used in the bioactivity assay. Cyclophosphamideinduced male Sprague Dawley rats were used as animal model and administered with rhG-CSF. Blood sample was collected at several points of time, before and after rhG-CSF treatments. Complete blood count and peripheral blood smear were conducted to investigate the activity of the rhG-CSF on each blood cells type, particularly neutrophil. Results: Specific activity on neutrophil proliferation was shown after treatments with our rhG-CSF and positive control. Positive control dose 40 mg/kg BW was statistically similar with that of the rhG-CSF dose 80 and 120 mg/kg BW. However, in neutropenic condition, recovery of neutrophil counts could not be achieved within 4 days of treatments. Thus, a longer treatment is needed to observe the activity of the rhG-CSF as an antineutropenia agent. Conclusion: The rhG-CSF has been proven having specific activity on neutrophil proliferation. 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