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data-broccoli-component="user-info.coauthors-count" data-click-track="profile-expand-user-info-coauthors"><p class="label">Co-authors</p><p class="data">12</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="50682354" href="https://www.academia.edu/Documents/in/Environmental_Pollution_and_Control_Technology"><div id="js-react-on-rails-context" style="display:none" 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data-props="{"color":"gray","children":["Dendritic Cells"]}" data-trace="false" data-dom-id="Pill-react-component-0a7e3ae5-2aaa-4e53-8197-3a28f31c04b0"></div> <div id="Pill-react-component-0a7e3ae5-2aaa-4e53-8197-3a28f31c04b0"></div> </a><a data-click-track="profile-user-info-expand-research-interests" data-has-card-for-ri-list="50682354" href="https://www.academia.edu/Documents/in/Cell_Differentiation"><div class="js-react-on-rails-component" style="display:none" data-component-name="Pill" data-props="{"color":"gray","children":["Cell Differentiation"]}" data-trace="false" data-dom-id="Pill-react-component-e194abe6-e240-4219-b9db-d1b8206b8424"></div> <div id="Pill-react-component-e194abe6-e240-4219-b9db-d1b8206b8424"></div> </a><a data-click-track="profile-user-info-expand-research-interests" data-has-card-for-ri-list="50682354" href="https://www.academia.edu/Documents/in/Polymerase_Chain_Reaction"><div class="js-react-on-rails-component" style="display:none" data-component-name="Pill" data-props="{"color":"gray","children":["Polymerase Chain Reaction"]}" data-trace="false" data-dom-id="Pill-react-component-44de6220-3921-4512-bad7-4a28080cd992"></div> <div id="Pill-react-component-44de6220-3921-4512-bad7-4a28080cd992"></div> </a><a data-click-track="profile-user-info-expand-research-interests" data-has-card-for-ri-list="50682354" href="https://www.academia.edu/Documents/in/Glycoproteins"><div class="js-react-on-rails-component" style="display:none" data-component-name="Pill" data-props="{"color":"gray","children":["Glycoproteins"]}" data-trace="false" data-dom-id="Pill-react-component-db3f07f1-2dd4-4903-aab4-a9c550c7c9fb"></div> <div id="Pill-react-component-db3f07f1-2dd4-4903-aab4-a9c550c7c9fb"></div> </a></div></div></div></div><div class="right-panel-container"><div class="user-content-wrapper"><div class="uploads-container" id="social-redesign-work-container"><div class="upload-header"><h2 class="ds2-5-heading-sans-serif-xs">Uploads</h2></div><div class="documents-container backbone-social-profile-documents" style="width: 100%;"><div class="u-taCenter"></div><div class="profile--tab_content_container js-tab-pane tab-pane active" id="all"><div class="profile--tab_heading_container js-section-heading" data-section="Papers" id="Papers"><h3 class="profile--tab_heading_container">Papers by Mahmood Jeddi-tehrani</h3></div><div class="js-work-strip profile--work_container" data-work-id="123639765"><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/123639765/Immunoreactivity_of_the_Cancer_Patients_Sera_Against_the_Purified_Recombinant_Nucleolin"><img alt="Research paper thumbnail of Immunoreactivity of the Cancer Patients' Sera Against the Purified Recombinant Nucleolin" 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/123639765/Immunoreactivity_of_the_Cancer_Patients_Sera_Against_the_Purified_Recombinant_Nucleolin">Immunoreactivity of the Cancer Patients' Sera Against the Purified Recombinant Nucleolin</a></div><div class="wp-workCard_item"><span>Social Science Research Network</span><span>, 2022</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="123639765"><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="123639765"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639765; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639765]").text(description); $(".js-view-count[data-work-id=123639765]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639765; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639765']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + 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href="https://www.academia.edu/123639764/Molecular_Study_on_Frequency_of_Single_Nucleotide_Polymorphism_of_TP53_Gene_among_Iranian_Patients_with_Gastric_Cancer"><img alt="Research paper thumbnail of Molecular Study on Frequency of Single Nucleotide Polymorphism of TP53 Gene among Iranian Patients with Gastric Cancer" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" rel="nofollow" href="https://www.academia.edu/123639764/Molecular_Study_on_Frequency_of_Single_Nucleotide_Polymorphism_of_TP53_Gene_among_Iranian_Patients_with_Gastric_Cancer">Molecular Study on Frequency of Single Nucleotide Polymorphism of TP53 Gene among Iranian Patients with Gastric Cancer</a></div><div class="wp-workCard_item"><span>American Journal of Gastroenterology</span><span>, 2005</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="123639764"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="123639764"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639764; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639764]").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" } } $('.js-work-strip[data-work-id=123639764]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639764,"title":"Molecular Study on Frequency of Single Nucleotide Polymorphism of TP53 Gene among Iranian Patients with Gastric Cancer","translated_title":"","metadata":{"publisher":"Ovid Technologies (Wolters Kluwer Health)","publication_date":{"day":null,"month":null,"year":2005,"errors":{}},"publication_name":"American Journal of 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href="https://www.academia.edu/123639763/_Production_and_characterization_of_monoclonal_antibodies_against_allergen_components_"><img alt="Research paper thumbnail of [Production and characterization of monoclonal antibodies against allergen components]" 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/123639763/_Production_and_characterization_of_monoclonal_antibodies_against_allergen_components_">[Production and characterization of monoclonal antibodies against allergen components]</a></div><div class="wp-workCard_item"><span>Immunität und Infektion</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">ABSTRACT</span></div><div class="wp-workCard_item wp-workCard--actions"><span 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href="https://www.academia.edu/123639762/Ligation_of_human_Fc_receptor_like_2_FCRL2_by_specific_monoclonal_antibodies_downregulates_B_cell_receptor_mediated_signaling">Ligation of human Fc receptor like-2 (FCRL2) by specific monoclonal antibodies downregulates B cell receptor mediated signaling</a></div><div class="wp-workCard_item"><span>Frontiers in Immunology</span><span>, 2013</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="123639762"><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 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href="https://www.academia.edu/123639761/Purification_of_inhibin_from_human_follicular_fluid_using_monoclonal_antibody"><img alt="Research paper thumbnail of Purification of inhibin from human follicular fluid using monoclonal antibody" 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" rel="nofollow" href="https://www.academia.edu/123639761/Purification_of_inhibin_from_human_follicular_fluid_using_monoclonal_antibody">Purification of inhibin from human follicular fluid using monoclonal antibody</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">PURIFICATION OF INHIBIN FROM HUMAN FOLLICULAR FLUID USING MONOCLONAL ANTIBODY SADEGHI MR*,HOJAT M...</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">PURIFICATION OF INHIBIN FROM HUMAN FOLLICULAR FLUID USING MONOCLONAL ANTIBODY SADEGHI MR*,HOJAT MAHSHID,NASERI NIMA,JEDI TEHRANI MAHMOUD,MOSAFANARIMAN,AKHOUNDI MOHAMMAD MAHDI,GHODS R.,BAYAT AA * DEPARTMENT OF ...</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="123639761"><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 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class="js-work-strip profile--work_container" data-work-id="123639723"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" rel="nofollow" href="https://www.academia.edu/123639723/Comparison_of_different_transient_gene_expression_systems_for_the_production_of_a_new_humanized_anti_HER2_monoclonal_antibody_Hersintuzumab_"><img alt="Research paper thumbnail of Comparison of different transient gene expression systems for the production of a new humanized anti-HER2 monoclonal antibody (Hersintuzumab)" 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" rel="nofollow" href="https://www.academia.edu/123639723/Comparison_of_different_transient_gene_expression_systems_for_the_production_of_a_new_humanized_anti_HER2_monoclonal_antibody_Hersintuzumab_">Comparison of different transient gene expression systems for the production of a new humanized anti-HER2 monoclonal antibody (Hersintuzumab)</a></div><div class="wp-workCard_item"><span>DARU Journal of Pharmaceutical Sciences</span><span>, Sep 10, 2023</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="123639723"><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 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container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639723, 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" } } $('.js-work-strip[data-work-id=123639723]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639723,"title":"Comparison of different transient gene expression systems for the production of a new humanized anti-HER2 monoclonal antibody (Hersintuzumab)","translated_title":"","metadata":{"publisher":"Springer Nature","publication_date":{"day":10,"month":9,"year":2023,"errors":{}},"publication_name":"DARU Journal of Pharmaceutical Sciences"},"translated_abstract":null,"internal_url":"https://www.academia.edu/123639723/Comparison_of_different_transient_gene_expression_systems_for_the_production_of_a_new_humanized_anti_HER2_monoclonal_antibody_Hersintuzumab_","translated_internal_url":"","created_at":"2024-09-07T04:35:00.451-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Comparison_of_different_transient_gene_expression_systems_for_the_production_of_a_new_humanized_anti_HER2_monoclonal_antibody_Hersintuzumab_","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics"},{"id":523,"name":"Chemistry","url":"https://www.academia.edu/Documents/in/Chemistry"},{"id":1290,"name":"Immunology","url":"https://www.academia.edu/Documents/in/Immunology"},{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":6599,"name":"Flow Cytometry","url":"https://www.academia.edu/Documents/in/Flow_Cytometry"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":37782,"name":"Cell Culture","url":"https://www.academia.edu/Documents/in/Cell_Culture"},{"id":357811,"name":"Antibody","url":"https://www.academia.edu/Documents/in/Antibody"},{"id":620070,"name":"Transfection","url":"https://www.academia.edu/Documents/in/Transfection"},{"id":766014,"name":"Monoclonal Antibody","url":"https://www.academia.edu/Documents/in/Monoclonal_Antibody"}],"urls":[{"id":44518696,"url":"https://doi.org/10.1007/s40199-023-00477-9"}]}, 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="123639722"><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/123639722/Expression_Purification_and_Characterization_of_Three_Overlapping_Immunodominant_Recombinant_Fragments_from_Bordetella_pertussis_Filamentous_Hemagglutinin"><img alt="Research paper thumbnail of Expression, Purification and Characterization of Three Overlapping Immunodominant Recombinant Fragments from Bordetella pertussis Filamentous Hemagglutinin" 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/123639722/Expression_Purification_and_Characterization_of_Three_Overlapping_Immunodominant_Recombinant_Fragments_from_Bordetella_pertussis_Filamentous_Hemagglutinin">Expression, Purification and Characterization of Three Overlapping Immunodominant Recombinant Fragments from Bordetella pertussis Filamentous Hemagglutinin</a></div><div class="wp-workCard_item"><span>PubMed</span><span>, 2013</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background: Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigen...</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">Background: Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigens of Bordetella pertussis (B. pertussis) and a major component of the acellular pertussis vaccine. In the present study, three overlapping recombinant fragments from the immunodominant region of FHA were produced and their immunogenicity was investigated. Methods: Three overlapping coding sequences of FHA antigen were amplified from B. pertussis genomic DNA by PCR. Amplified fragments were expressed in Escherichia coli (E. coli) BL21(DE3) strain and purified through His-tag using Nickel-based chromatography. Purified fragments were characterized by SDS-PAGE and Western blotting techniques. In vitro peripheral blood mononuclear cells (PBMC) proliferation and IFN-γ production were assessed in a limited number of healthy adults vaccinated with a commercial acellular pertussis vaccine in response to all purified FHA fragments by H3-Thymidine incorporation and ELISA, respectively. Results: Recombinant FHA segments were successfully cloned and produced at high levels in E. coli BL21(DE3). SDS-PAGE and Western blot analyses confirmed their purity and reactivity. All three recombinant fragments together with a commercial native FHA were able to induce in vitro PBMC proliferation and IFN-γ production. Conclusion: Our preliminary results suggest that these overlapping recombinant FHA fragments are immunogenic and may prove to be immuno-protective.</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="123639722"><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="123639722"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639722; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639722]").text(description); $(".js-view-count[data-work-id=123639722]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639722; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639722']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639722, 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" } } $('.js-work-strip[data-work-id=123639722]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639722,"title":"Expression, Purification and Characterization of Three Overlapping Immunodominant Recombinant Fragments from Bordetella pertussis Filamentous Hemagglutinin","translated_title":"","metadata":{"abstract":"Background: Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigens of Bordetella pertussis (B. pertussis) and a major component of the acellular pertussis vaccine. In the present study, three overlapping recombinant fragments from the immunodominant region of FHA were produced and their immunogenicity was investigated. Methods: Three overlapping coding sequences of FHA antigen were amplified from B. pertussis genomic DNA by PCR. Amplified fragments were expressed in Escherichia coli (E. coli) BL21(DE3) strain and purified through His-tag using Nickel-based chromatography. Purified fragments were characterized by SDS-PAGE and Western blotting techniques. In vitro peripheral blood mononuclear cells (PBMC) proliferation and IFN-γ production were assessed in a limited number of healthy adults vaccinated with a commercial acellular pertussis vaccine in response to all purified FHA fragments by H3-Thymidine incorporation and ELISA, respectively. Results: Recombinant FHA segments were successfully cloned and produced at high levels in E. coli BL21(DE3). SDS-PAGE and Western blot analyses confirmed their purity and reactivity. All three recombinant fragments together with a commercial native FHA were able to induce in vitro PBMC proliferation and IFN-γ production. Conclusion: Our preliminary results suggest that these overlapping recombinant FHA fragments are immunogenic and may prove to be immuno-protective.","publication_date":{"day":null,"month":null,"year":2013,"errors":{}},"publication_name":"PubMed"},"translated_abstract":"Background: Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigens of Bordetella pertussis (B. pertussis) and a major component of the acellular pertussis vaccine. In the present study, three overlapping recombinant fragments from the immunodominant region of FHA were produced and their immunogenicity was investigated. Methods: Three overlapping coding sequences of FHA antigen were amplified from B. pertussis genomic DNA by PCR. Amplified fragments were expressed in Escherichia coli (E. coli) BL21(DE3) strain and purified through His-tag using Nickel-based chromatography. Purified fragments were characterized by SDS-PAGE and Western blotting techniques. In vitro peripheral blood mononuclear cells (PBMC) proliferation and IFN-γ production were assessed in a limited number of healthy adults vaccinated with a commercial acellular pertussis vaccine in response to all purified FHA fragments by H3-Thymidine incorporation and ELISA, respectively. Results: Recombinant FHA segments were successfully cloned and produced at high levels in E. coli BL21(DE3). SDS-PAGE and Western blot analyses confirmed their purity and reactivity. All three recombinant fragments together with a commercial native FHA were able to induce in vitro PBMC proliferation and IFN-γ production. Conclusion: Our preliminary results suggest that these overlapping recombinant FHA fragments are immunogenic and may prove to be immuno-protective.","internal_url":"https://www.academia.edu/123639722/Expression_Purification_and_Characterization_of_Three_Overlapping_Immunodominant_Recombinant_Fragments_from_Bordetella_pertussis_Filamentous_Hemagglutinin","translated_internal_url":"","created_at":"2024-09-07T04:35:00.228-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Expression_Purification_and_Characterization_of_Three_Overlapping_Immunodominant_Recombinant_Fragments_from_Bordetella_pertussis_Filamentous_Hemagglutinin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":159,"name":"Microbiology","url":"https://www.academia.edu/Documents/in/Microbiology"},{"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":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":98939,"name":"Pubmed","url":"https://www.academia.edu/Documents/in/Pubmed"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":1314192,"name":"Immunogenicity","url":"https://www.academia.edu/Documents/in/Immunogenicity"},{"id":1714726,"name":"Bordetella Pertussis","url":"https://www.academia.edu/Documents/in/Bordetella_Pertussis"}],"urls":[{"id":44518695,"url":"https://pubmed.ncbi.nlm.nih.gov/23626873"}]}, 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="123639721"><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/123639721/Production_and_characterization_of_polyclonal_antibody_against_a_synthetic_peptide_from_%CE%B2_actin_protein"><img alt="Research paper thumbnail of Production and characterization of polyclonal antibody against a synthetic peptide from β-actin protein" 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/123639721/Production_and_characterization_of_polyclonal_antibody_against_a_synthetic_peptide_from_%CE%B2_actin_protein">Production and characterization of polyclonal antibody against a synthetic peptide from β-actin protein</a></div><div class="wp-workCard_item"><span>PubMed</span><span>, Jun 1, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Objectives: Antibodies against actin, as one of the most widely studied structural and multifunct...</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">Objectives: Antibodies against actin, as one of the most widely studied structural and multifunctional housekeeping proteins in eukaryotic cells, are used as internal loading controls in western blot analyses. The aim of this study was to produce polyclonal antibody against a synthetic peptide derived from N-terminal region of β-actin protein to be used as a protein loading control in western blot and other assay systems. Materials and methods: A synthetic peptide derived from β-actin protein was designed and conjugated to Keyhole limpet hemocyanin (KLH) and used to immunize a white New Zealand rabbit. The antibody was purified from serum by affinity chromatography column. The purity of the antibody was determined by SDS-PAGE and its ability to recognize the immunizing peptide was measured by ELISA. The reactivity of the antibody with β-actin protein in a panel of different cell lysates was then evaluated by western blot. In addition, the reactivity of the antibody with the corresponding protein was also evaluated by Immunocytochemistry and Immunohistochemistry in different samples. Results: The antibody could recognize the immunizing peptide in ELISA. It could also recognize β-actin protein in western blot as well as in immunocytochemistry and immunohistochemistry. Conclusion: Our data suggest that this antibody may be used as an internal control in western blot analyses as well as in other immunological applications such as ELISA, immunocytochemistry and immunohistochemistry.</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="123639721"><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="123639721"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639721; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639721]").text(description); $(".js-view-count[data-work-id=123639721]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639721; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639721']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639721, 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" } } $('.js-work-strip[data-work-id=123639721]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639721,"title":"Production and characterization of polyclonal antibody against a synthetic peptide from β-actin protein","translated_title":"","metadata":{"abstract":"Objectives: Antibodies against actin, as one of the most widely studied structural and multifunctional housekeeping proteins in eukaryotic cells, are used as internal loading controls in western blot analyses. The aim of this study was to produce polyclonal antibody against a synthetic peptide derived from N-terminal region of β-actin protein to be used as a protein loading control in western blot and other assay systems. Materials and methods: A synthetic peptide derived from β-actin protein was designed and conjugated to Keyhole limpet hemocyanin (KLH) and used to immunize a white New Zealand rabbit. The antibody was purified from serum by affinity chromatography column. The purity of the antibody was determined by SDS-PAGE and its ability to recognize the immunizing peptide was measured by ELISA. The reactivity of the antibody with β-actin protein in a panel of different cell lysates was then evaluated by western blot. In addition, the reactivity of the antibody with the corresponding protein was also evaluated by Immunocytochemistry and Immunohistochemistry in different samples. Results: The antibody could recognize the immunizing peptide in ELISA. It could also recognize β-actin protein in western blot as well as in immunocytochemistry and immunohistochemistry. Conclusion: Our data suggest that this antibody may be used as an internal control in western blot analyses as well as in other immunological applications such as ELISA, immunocytochemistry and immunohistochemistry.","publication_date":{"day":1,"month":6,"year":2014,"errors":{}},"publication_name":"PubMed"},"translated_abstract":"Objectives: Antibodies against actin, as one of the most widely studied structural and multifunctional housekeeping proteins in eukaryotic cells, are used as internal loading controls in western blot analyses. The aim of this study was to produce polyclonal antibody against a synthetic peptide derived from N-terminal region of β-actin protein to be used as a protein loading control in western blot and other assay systems. Materials and methods: A synthetic peptide derived from β-actin protein was designed and conjugated to Keyhole limpet hemocyanin (KLH) and used to immunize a white New Zealand rabbit. The antibody was purified from serum by affinity chromatography column. The purity of the antibody was determined by SDS-PAGE and its ability to recognize the immunizing peptide was measured by ELISA. The reactivity of the antibody with β-actin protein in a panel of different cell lysates was then evaluated by western blot. In addition, the reactivity of the antibody with the corresponding protein was also evaluated by Immunocytochemistry and Immunohistochemistry in different samples. Results: The antibody could recognize the immunizing peptide in ELISA. It could also recognize β-actin protein in western blot as well as in immunocytochemistry and immunohistochemistry. Conclusion: Our data suggest that this antibody may be used as an internal control in western blot analyses as well as in other immunological applications such as ELISA, immunocytochemistry and immunohistochemistry.","internal_url":"https://www.academia.edu/123639721/Production_and_characterization_of_polyclonal_antibody_against_a_synthetic_peptide_from_%CE%B2_actin_protein","translated_internal_url":"","created_at":"2024-09-07T04:35:00.014-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Production_and_characterization_of_polyclonal_antibody_against_a_synthetic_peptide_from_β_actin_protein","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":12071,"name":"Immunohistochemistry","url":"https://www.academia.edu/Documents/in/Immunohistochemistry"},{"id":37895,"name":"Immunocytochemistry","url":"https://www.academia.edu/Documents/in/Immunocytochemistry"},{"id":98939,"name":"Pubmed","url":"https://www.academia.edu/Documents/in/Pubmed"},{"id":201296,"name":"Peptide","url":"https://www.academia.edu/Documents/in/Peptide"},{"id":357811,"name":"Antibody","url":"https://www.academia.edu/Documents/in/Antibody"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":470726,"name":"Polyclonal Antibodies","url":"https://www.academia.edu/Documents/in/Polyclonal_Antibodies"}],"urls":[{"id":44518694,"url":"https://pubmed.ncbi.nlm.nih.gov/25140199"}]}, 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="123639720"><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/123639720/Production_and_characterization_of_a_murine_monoclonal_antibody_against_human_ferritin"><img alt="Research paper thumbnail of Production and characterization of a murine monoclonal antibody against human ferritin" 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/123639720/Production_and_characterization_of_a_murine_monoclonal_antibody_against_human_ferritin">Production and characterization of a murine monoclonal antibody against human ferritin</a></div><div class="wp-workCard_item"><span>PubMed</span><span>, Oct 1, 2013</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background: Ferritin is an iron storage protein, which plays a key role in iron metabolism. Measu...</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">Background: Ferritin is an iron storage protein, which plays a key role in iron metabolism. Measurement of ferritin level in serum is one of the most useful indicators of iron status and also a sensitive measurement of iron deficiency. Monoclonal antibodies may be useful as a tool in various aspects of ferritin investigations. In this paper, the production of a murine monoclonal antibody (mAb) against human ferritin was reported. Methods: Balb/c mice were immunized with purified human ferritin and splenocytes of hyper immunized mice were fused with Sp2/0 myeloma cells. After four times of cloning by limiting dilution, a positive hybridoma (clone: 2F9-C9) was selected by ELISA using human ferritin. Anti-ferritin mAb was purified from culture supernatants by affinity chromatography. Results: Determination of the antibody affinity for ferritin by ELISA revealed a relatively high affinity (2.34×10(9) M (-1)) and the isotype was determined to be IgG2a. The anti-ferritin mAb 2F9-C9 reacted with 79.4% of Hela cells in flow cytometry. The antibody detected a band of 20 kDa in K562 cells, murine and human liver lysates, purified ferritin in Western blot and also ferritin in human serum. Conclusion: This mAb can specifically recognize ferritin and may serve as a component of ferritin diagnostic kit if other requirements of the kit are met.</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="123639720"><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="123639720"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639720; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639720]").text(description); $(".js-view-count[data-work-id=123639720]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639720; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639720']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639720, 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" } } $('.js-work-strip[data-work-id=123639720]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639720,"title":"Production and characterization of a murine monoclonal antibody against human ferritin","translated_title":"","metadata":{"abstract":"Background: Ferritin is an iron storage protein, which plays a key role in iron metabolism. Measurement of ferritin level in serum is one of the most useful indicators of iron status and also a sensitive measurement of iron deficiency. Monoclonal antibodies may be useful as a tool in various aspects of ferritin investigations. In this paper, the production of a murine monoclonal antibody (mAb) against human ferritin was reported. Methods: Balb/c mice were immunized with purified human ferritin and splenocytes of hyper immunized mice were fused with Sp2/0 myeloma cells. After four times of cloning by limiting dilution, a positive hybridoma (clone: 2F9-C9) was selected by ELISA using human ferritin. Anti-ferritin mAb was purified from culture supernatants by affinity chromatography. Results: Determination of the antibody affinity for ferritin by ELISA revealed a relatively high affinity (2.34×10(9) M (-1)) and the isotype was determined to be IgG2a. The anti-ferritin mAb 2F9-C9 reacted with 79.4% of Hela cells in flow cytometry. The antibody detected a band of 20 kDa in K562 cells, murine and human liver lysates, purified ferritin in Western blot and also ferritin in human serum. Conclusion: This mAb can specifically recognize ferritin and may serve as a component of ferritin diagnostic kit if other requirements of the kit are met.","publication_date":{"day":1,"month":10,"year":2013,"errors":{}},"publication_name":"PubMed"},"translated_abstract":"Background: Ferritin is an iron storage protein, which plays a key role in iron metabolism. Measurement of ferritin level in serum is one of the most useful indicators of iron status and also a sensitive measurement of iron deficiency. Monoclonal antibodies may be useful as a tool in various aspects of ferritin investigations. In this paper, the production of a murine monoclonal antibody (mAb) against human ferritin was reported. Methods: Balb/c mice were immunized with purified human ferritin and splenocytes of hyper immunized mice were fused with Sp2/0 myeloma cells. After four times of cloning by limiting dilution, a positive hybridoma (clone: 2F9-C9) was selected by ELISA using human ferritin. Anti-ferritin mAb was purified from culture supernatants by affinity chromatography. Results: Determination of the antibody affinity for ferritin by ELISA revealed a relatively high affinity (2.34×10(9) M (-1)) and the isotype was determined to be IgG2a. The anti-ferritin mAb 2F9-C9 reacted with 79.4% of Hela cells in flow cytometry. The antibody detected a band of 20 kDa in K562 cells, murine and human liver lysates, purified ferritin in Western blot and also ferritin in human serum. Conclusion: This mAb can specifically recognize ferritin and may serve as a component of ferritin diagnostic kit if other requirements of the kit are met.","internal_url":"https://www.academia.edu/123639720/Production_and_characterization_of_a_murine_monoclonal_antibody_against_human_ferritin","translated_internal_url":"","created_at":"2024-09-07T04:34:59.748-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Production_and_characterization_of_a_murine_monoclonal_antibody_against_human_ferritin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":98939,"name":"Pubmed","url":"https://www.academia.edu/Documents/in/Pubmed"},{"id":201241,"name":"Affinity chromatography","url":"https://www.academia.edu/Documents/in/Affinity_chromatography"},{"id":220230,"name":"Ferritin","url":"https://www.academia.edu/Documents/in/Ferritin"},{"id":357811,"name":"Antibody","url":"https://www.academia.edu/Documents/in/Antibody"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":766014,"name":"Monoclonal Antibody","url":"https://www.academia.edu/Documents/in/Monoclonal_Antibody"}],"urls":[{"id":44518693,"url":"https://pubmed.ncbi.nlm.nih.gov/24285995"}]}, 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="123639718"><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/123639718/Extraction_Purification_and_Characterization_of_Lipopolysaccharide_from_Escherichia_coli_and_Salmonella_typhi"><img alt="Research paper thumbnail of Extraction, Purification and Characterization of Lipopolysaccharide from Escherichia coli and Salmonella typhi" 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/123639718/Extraction_Purification_and_Characterization_of_Lipopolysaccharide_from_Escherichia_coli_and_Salmonella_typhi">Extraction, Purification and Characterization of Lipopolysaccharide from Escherichia coli and Salmonella typhi</a></div><div class="wp-workCard_item"><span>PubMed</span><span>, 2011</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Lipopolysaccharide (LPS) is an important structural component of the outer cell membrane complex ...</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">Lipopolysaccharide (LPS) is an important structural component of the outer cell membrane complex of gram negative microorganisms. Its causative role in gram negative bacteria-induced diseases and broad applications in different kinds of cell stimulation experiments provided a conceptual basis for studies directed at the isolation, purification, and detailed chemical characterization of LPS. The main problem with LPS purification protocols is the contamination of the end product with nucleic acids and proteins in variable proportions which could potentially interfere with downstream applications. In this study, a simple procedure for purification of LPS from Escherichia coli (E.coli) and Salmonella typhi (S.typhi) with high purity and very low contaminating nucleic acids and proteins based on the hot phenol-water extraction protocol has been introduced. The purity of extracted LPS was evaluated by silver and coomassie blue staining of SDS-PAGE gels and HPLC analysis. Limulus Amebocyte Lysate (LAL) coagulation activity and rabbit pyrogen assay were exploited to monitor the functionality of purified LPS. The results showed that DNase and RNase treatment of the sample is essential after the sonication step to eliminate nucleic acid contamination in the LPS fraction. Silver staining demonstrated ladder pattern which is characteristic of LPS. No contaminating protein was found as assessed by coomassie blue staining. HPLC fractionation revealed high degree of purity comparable with commercial LPS. Parenteral administration of purified LPS resulted in substantial increase of rabbits' body temperature (mean: 1.45°C). LAL coagulation assay confirmed the functional activity of the purified LPS. In conclusion, the protocol presented here could be employed for isolation of LPS with high purity and functional activity.</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="123639718"><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="123639718"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639718; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639718]").text(description); $(".js-view-count[data-work-id=123639718]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639718; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639718']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639718, 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" } } $('.js-work-strip[data-work-id=123639718]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639718,"title":"Extraction, Purification and Characterization of Lipopolysaccharide from Escherichia coli and Salmonella typhi","translated_title":"","metadata":{"abstract":"Lipopolysaccharide (LPS) is an important structural component of the outer cell membrane complex of gram negative microorganisms. Its causative role in gram negative bacteria-induced diseases and broad applications in different kinds of cell stimulation experiments provided a conceptual basis for studies directed at the isolation, purification, and detailed chemical characterization of LPS. The main problem with LPS purification protocols is the contamination of the end product with nucleic acids and proteins in variable proportions which could potentially interfere with downstream applications. In this study, a simple procedure for purification of LPS from Escherichia coli (E.coli) and Salmonella typhi (S.typhi) with high purity and very low contaminating nucleic acids and proteins based on the hot phenol-water extraction protocol has been introduced. The purity of extracted LPS was evaluated by silver and coomassie blue staining of SDS-PAGE gels and HPLC analysis. Limulus Amebocyte Lysate (LAL) coagulation activity and rabbit pyrogen assay were exploited to monitor the functionality of purified LPS. The results showed that DNase and RNase treatment of the sample is essential after the sonication step to eliminate nucleic acid contamination in the LPS fraction. Silver staining demonstrated ladder pattern which is characteristic of LPS. No contaminating protein was found as assessed by coomassie blue staining. HPLC fractionation revealed high degree of purity comparable with commercial LPS. Parenteral administration of purified LPS resulted in substantial increase of rabbits' body temperature (mean: 1.45°C). LAL coagulation assay confirmed the functional activity of the purified LPS. In conclusion, the protocol presented here could be employed for isolation of LPS with high purity and functional activity.","publication_date":{"day":null,"month":null,"year":2011,"errors":{}},"publication_name":"PubMed"},"translated_abstract":"Lipopolysaccharide (LPS) is an important structural component of the outer cell membrane complex of gram negative microorganisms. Its causative role in gram negative bacteria-induced diseases and broad applications in different kinds of cell stimulation experiments provided a conceptual basis for studies directed at the isolation, purification, and detailed chemical characterization of LPS. The main problem with LPS purification protocols is the contamination of the end product with nucleic acids and proteins in variable proportions which could potentially interfere with downstream applications. In this study, a simple procedure for purification of LPS from Escherichia coli (E.coli) and Salmonella typhi (S.typhi) with high purity and very low contaminating nucleic acids and proteins based on the hot phenol-water extraction protocol has been introduced. The purity of extracted LPS was evaluated by silver and coomassie blue staining of SDS-PAGE gels and HPLC analysis. Limulus Amebocyte Lysate (LAL) coagulation activity and rabbit pyrogen assay were exploited to monitor the functionality of purified LPS. The results showed that DNase and RNase treatment of the sample is essential after the sonication step to eliminate nucleic acid contamination in the LPS fraction. Silver staining demonstrated ladder pattern which is characteristic of LPS. No contaminating protein was found as assessed by coomassie blue staining. HPLC fractionation revealed high degree of purity comparable with commercial LPS. Parenteral administration of purified LPS resulted in substantial increase of rabbits' body temperature (mean: 1.45°C). LAL coagulation assay confirmed the functional activity of the purified LPS. In conclusion, the protocol presented here could be employed for isolation of LPS with high purity and functional activity.","internal_url":"https://www.academia.edu/123639718/Extraction_Purification_and_Characterization_of_Lipopolysaccharide_from_Escherichia_coli_and_Salmonella_typhi","translated_internal_url":"","created_at":"2024-09-07T04:34:58.638-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Extraction_Purification_and_Characterization_of_Lipopolysaccharide_from_Escherichia_coli_and_Salmonella_typhi","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":48183,"name":"Lipopolysaccharide","url":"https://www.academia.edu/Documents/in/Lipopolysaccharide"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":98939,"name":"Pubmed","url":"https://www.academia.edu/Documents/in/Pubmed"},{"id":1256745,"name":"Lysis","url":"https://www.academia.edu/Documents/in/Lysis"},{"id":1727314,"name":"Nucleic Acid","url":"https://www.academia.edu/Documents/in/Nucleic_Acid"}],"urls":[{"id":44518691,"url":"https://pubmed.ncbi.nlm.nih.gov/23407691"}]}, 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="123639717"><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/123639717/Proteome_Analysis_of_Adult_Acute_Lymphoblastic_Leukemia_by_Two_dimensional_Blue_Native_Sodium_Dodecyl_Sulfate_Gel_Electrophoresis"><img alt="Research paper thumbnail of Proteome Analysis of Adult Acute Lymphoblastic Leukemia by Two-dimensional Blue Native/Sodium Dodecyl Sulfate Gel Electrophoresis" 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/123639717/Proteome_Analysis_of_Adult_Acute_Lymphoblastic_Leukemia_by_Two_dimensional_Blue_Native_Sodium_Dodecyl_Sulfate_Gel_Electrophoresis">Proteome Analysis of Adult Acute Lymphoblastic Leukemia by Two-dimensional Blue Native/Sodium Dodecyl Sulfate Gel Electrophoresis</a></div><div class="wp-workCard_item"><span>Avicenna journal of medical biotechnology</span><span>, Dec 20, 2022</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background:Despite the significant progress in the treatment of Acute Lymphoblastic Leukemia (ALL...</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">Background:Despite the significant progress in the treatment of Acute Lymphoblastic Leukemia (ALL) in children, it still remains as one of the most challenging malignancies in adults. Identification of new biomarkers may improve the management of adult ALL. Proteins expressed on the cell surface can be considered as disease-associated biomarkers with potential for diagnosis and targeted therapies. Thus, membrane proteome studies give essential information about the disease-related biomarkers.Methods:We applied 2-dimensional blue-native SDS-PAGE technique followed by MALDI-TOF/TOF-mass spectrometry to study the cell membrane proteome of peripheral blood mononuclear cells of adult B-ALL patients in comparison to that of the healthy controls.Results:Sixty seven differentially expressed protein spots were detected, among them 52 proteins were found to be up-regulated but the other 15 proteins were down-regulated in B-ALL. Five differentially expressed proteins, involved in energy metabolism pathways, were detected in B-ALL patients compared to the healthy control group.Conclusion:Differentially expressed proteins provide an insight into the molecular biology of B-ALL. Further studies must be done to confirm our data to be considered as potential targets for detection and treatment of B-ALL.</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="123639717"><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="123639717"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639717; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639717]").text(description); $(".js-view-count[data-work-id=123639717]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639717; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639717']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639717, 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" } } $('.js-work-strip[data-work-id=123639717]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639717,"title":"Proteome Analysis of Adult Acute Lymphoblastic Leukemia by Two-dimensional Blue Native/Sodium Dodecyl Sulfate Gel Electrophoresis","translated_title":"","metadata":{"abstract":"Background:Despite the significant progress in the treatment of Acute Lymphoblastic Leukemia (ALL) in children, it still remains as one of the most challenging malignancies in adults. Identification of new biomarkers may improve the management of adult ALL. Proteins expressed on the cell surface can be considered as disease-associated biomarkers with potential for diagnosis and targeted therapies. Thus, membrane proteome studies give essential information about the disease-related biomarkers.Methods:We applied 2-dimensional blue-native SDS-PAGE technique followed by MALDI-TOF/TOF-mass spectrometry to study the cell membrane proteome of peripheral blood mononuclear cells of adult B-ALL patients in comparison to that of the healthy controls.Results:Sixty seven differentially expressed protein spots were detected, among them 52 proteins were found to be up-regulated but the other 15 proteins were down-regulated in B-ALL. Five differentially expressed proteins, involved in energy metabolism pathways, were detected in B-ALL patients compared to the healthy control group.Conclusion:Differentially expressed proteins provide an insight into the molecular biology of B-ALL. Further studies must be done to confirm our data to be considered as potential targets for detection and treatment of B-ALL.","publisher":"Knowledge E","publication_date":{"day":20,"month":12,"year":2022,"errors":{}},"publication_name":"Avicenna journal of medical biotechnology"},"translated_abstract":"Background:Despite the significant progress in the treatment of Acute Lymphoblastic Leukemia (ALL) in children, it still remains as one of the most challenging malignancies in adults. Identification of new biomarkers may improve the management of adult ALL. Proteins expressed on the cell surface can be considered as disease-associated biomarkers with potential for diagnosis and targeted therapies. Thus, membrane proteome studies give essential information about the disease-related biomarkers.Methods:We applied 2-dimensional blue-native SDS-PAGE technique followed by MALDI-TOF/TOF-mass spectrometry to study the cell membrane proteome of peripheral blood mononuclear cells of adult B-ALL patients in comparison to that of the healthy controls.Results:Sixty seven differentially expressed protein spots were detected, among them 52 proteins were found to be up-regulated but the other 15 proteins were down-regulated in B-ALL. Five differentially expressed proteins, involved in energy metabolism pathways, were detected in B-ALL patients compared to the healthy control group.Conclusion:Differentially expressed proteins provide an insight into the molecular biology of B-ALL. Further studies must be done to confirm our data to be considered as potential targets for detection and treatment of B-ALL.","internal_url":"https://www.academia.edu/123639717/Proteome_Analysis_of_Adult_Acute_Lymphoblastic_Leukemia_by_Two_dimensional_Blue_Native_Sodium_Dodecyl_Sulfate_Gel_Electrophoresis","translated_internal_url":"","created_at":"2024-09-07T04:34:57.195-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Proteome_Analysis_of_Adult_Acute_Lymphoblastic_Leukemia_by_Two_dimensional_Blue_Native_Sodium_Dodecyl_Sulfate_Gel_Electrophoresis","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":759403,"name":"Gel electrophoresis","url":"https://www.academia.edu/Documents/in/Gel_electrophoresis"},{"id":1035050,"name":"Proteome","url":"https://www.academia.edu/Documents/in/Proteome"},{"id":2622517,"name":"Sodium Dodecyl Sulfate","url":"https://www.academia.edu/Documents/in/Sodium_Dodecyl_Sulfate"}],"urls":[{"id":44518690,"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9895978"}]}, 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="123639716"><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/123639716/Cloning_Expression_and_Characterization_of_a_Peptibody_To_Deplete_Myeloid_Derived_Suppressor_Cells_in_a_Murine_Mammary_Carcinoma_Model"><img alt="Research paper thumbnail of Cloning, Expression and Characterization of a Peptibody To Deplete Myeloid Derived Suppressor Cells in a Murine Mammary Carcinoma Model" class="work-thumbnail" src="https://attachments.academia-assets.com/118024543/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/123639716/Cloning_Expression_and_Characterization_of_a_Peptibody_To_Deplete_Myeloid_Derived_Suppressor_Cells_in_a_Murine_Mammary_Carcinoma_Model">Cloning, Expression and Characterization of a Peptibody To Deplete Myeloid Derived Suppressor Cells in a Murine Mammary Carcinoma Model</a></div><div class="wp-workCard_item"><span>Research Square (Research Square)</span><span>, Dec 28, 2021</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="5df65146b38fa450fb7bd4f07c88615f" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":118024543,"asset_id":123639716,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/118024543/download_file?st=MTczMjQzOTg0Nyw4LjIyMi4yMDguMTQ2&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="123639716"><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 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WowProfile.WorkStripView({ el: this, workJSON: {"id":123639716,"title":"Cloning, Expression and Characterization of a Peptibody To Deplete Myeloid Derived Suppressor Cells in a Murine Mammary Carcinoma Model","translated_title":"","metadata":{"publisher":"Research Square","publication_date":{"day":28,"month":12,"year":2021,"errors":{}},"publication_name":"Research Square (Research 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href="https://www.academia.edu/123639715/Immunogenicity_and_reactogenicity_of_two_diphtheria_tetanus_whole_cell_pertussis_vaccines_in_Iranian_pre_school_children_a_randomized_controlled_trial"><img alt="Research paper thumbnail of Immunogenicity and reactogenicity of two diphtheria-tetanus-whole cell pertussis vaccines in Iranian pre-school children, a randomized controlled trial" class="work-thumbnail" src="https://attachments.academia-assets.com/118024528/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/123639715/Immunogenicity_and_reactogenicity_of_two_diphtheria_tetanus_whole_cell_pertussis_vaccines_in_Iranian_pre_school_children_a_randomized_controlled_trial">Immunogenicity and reactogenicity of two diphtheria-tetanus-whole cell pertussis vaccines in Iranian pre-school children, a randomized controlled trial</a></div><div class="wp-workCard_item"><span>Human Vaccines & Immunotherapeutics</span><span>, Jun 12, 2013</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="9c130c498e561c651c2a89ff2f332560" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":118024528,"asset_id":123639715,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/118024528/download_file?st=MTczMjQzOTg0Nyw4LjIyMi4yMDguMTQ2&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="123639715"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa 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B","url":"https://www.academia.edu/Documents/in/Hepatitis_B"},{"id":64568,"name":"Humans","url":"https://www.academia.edu/Documents/in/Humans"},{"id":64933,"name":"Child","url":"https://www.academia.edu/Documents/in/Child"},{"id":98925,"name":"Female","url":"https://www.academia.edu/Documents/in/Female"},{"id":111545,"name":"Male","url":"https://www.academia.edu/Documents/in/Male"},{"id":134346,"name":"Infant","url":"https://www.academia.edu/Documents/in/Infant"},{"id":387144,"name":"Fever","url":"https://www.academia.edu/Documents/in/Fever"},{"id":453435,"name":"Hum","url":"https://www.academia.edu/Documents/in/Hum"},{"id":1272906,"name":"Enzyme Linked Immunosorbent Assay","url":"https://www.academia.edu/Documents/in/Enzyme_Linked_Immunosorbent_Assay"},{"id":1314192,"name":"Immunogenicity","url":"https://www.academia.edu/Documents/in/Immunogenicity"},{"id":1329331,"name":"Human Vaccines","url":"https://www.academia.edu/Documents/in/Human_Vaccines"},{"id":1529194,"name":"Hepatitis B Vaccines","url":"https://www.academia.edu/Documents/in/Hepatitis_B_Vaccines"},{"id":1817270,"name":"Diphtheria","url":"https://www.academia.edu/Documents/in/Diphtheria"},{"id":1990998,"name":"Haemophilus influenzae","url":"https://www.academia.edu/Documents/in/Haemophilus_influenzae"},{"id":2489700,"name":"Child preschool","url":"https://www.academia.edu/Documents/in/Child_preschool"}],"urls":[{"id":44518687,"url":"https://www.tandfonline.com/doi/pdf/10.4161/hv.24093?needAccess=true"}]}, 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="123639714"><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/123639714/Impact_of_regulatory_T_cell_therapy_on_immune_cell_composition_and_fetal_survival_rate_in_abortion_prone_mice"><img alt="Research paper thumbnail of Impact of regulatory T cell therapy on immune cell composition and fetal survival rate in abortion prone mice" 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/123639714/Impact_of_regulatory_T_cell_therapy_on_immune_cell_composition_and_fetal_survival_rate_in_abortion_prone_mice">Impact of regulatory T cell therapy on immune cell composition and fetal survival rate in abortion prone mice</a></div><div class="wp-workCard_item"><span>Reproduction, Fertility and Development</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Context Implantation of fertilised eggs and survival of a semi-allogenic embryo rely on the inter...</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">Context Implantation of fertilised eggs and survival of a semi-allogenic embryo rely on the interactions between the cells and molecules preparing the uterus. We investigated the effect of regulatory T cell (Treg) therapy on the mechanism of local immune tolerance of mice prone to spontaneous abortion. Methods Naive T cells were stimulated in vitro with 17β-oestradiol (E2), progesterone (P4) and TGF-β1 for 96 h to generate induced Tregs (iTreg). The iTregs were injected into DBA/2-mated pregnant CBA/J female mice (abortion prone model). On day 14 of pregnancy, mice were killed and decidual and placental tissues were collected for cellular composition analysis. Results Abortion prone mice (PBS treated) showed significantly lower survival rates (P &lt; 0.0001), increased CD3+CD8+ (P &lt; 0.05), lower IDO+ (P &lt; 0.05) and increased natural killer cells (uNK) cell numbers (P &lt; 0.001) in the uterus, as well increased NK cells in the placenta (P &lt; 0.05) than in normal pregnant mic...</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="123639714"><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="123639714"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639714; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639714]").text(description); $(".js-view-count[data-work-id=123639714]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639714; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639714']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639714, 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" } } $('.js-work-strip[data-work-id=123639714]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639714,"title":"Impact of regulatory T cell therapy on immune cell composition and fetal survival rate in abortion prone mice","translated_title":"","metadata":{"abstract":"Context Implantation of fertilised eggs and survival of a semi-allogenic embryo rely on the interactions between the cells and molecules preparing the uterus. We investigated the effect of regulatory T cell (Treg) therapy on the mechanism of local immune tolerance of mice prone to spontaneous abortion. Methods Naive T cells were stimulated in vitro with 17β-oestradiol (E2), progesterone (P4) and TGF-β1 for 96 h to generate induced Tregs (iTreg). The iTregs were injected into DBA/2-mated pregnant CBA/J female mice (abortion prone model). On day 14 of pregnancy, mice were killed and decidual and placental tissues were collected for cellular composition analysis. Results Abortion prone mice (PBS treated) showed significantly lower survival rates (P \u0026lt; 0.0001), increased CD3+CD8+ (P \u0026lt; 0.05), lower IDO+ (P \u0026lt; 0.05) and increased natural killer cells (uNK) cell numbers (P \u0026lt; 0.001) in the uterus, as well increased NK cells in the placenta (P \u0026lt; 0.05) than in normal pregnant mic...","publisher":"CSIRO Publishing","publication_name":"Reproduction, Fertility and Development"},"translated_abstract":"Context Implantation of fertilised eggs and survival of a semi-allogenic embryo rely on the interactions between the cells and molecules preparing the uterus. We investigated the effect of regulatory T cell (Treg) therapy on the mechanism of local immune tolerance of mice prone to spontaneous abortion. Methods Naive T cells were stimulated in vitro with 17β-oestradiol (E2), progesterone (P4) and TGF-β1 for 96 h to generate induced Tregs (iTreg). The iTregs were injected into DBA/2-mated pregnant CBA/J female mice (abortion prone model). On day 14 of pregnancy, mice were killed and decidual and placental tissues were collected for cellular composition analysis. Results Abortion prone mice (PBS treated) showed significantly lower survival rates (P \u0026lt; 0.0001), increased CD3+CD8+ (P \u0026lt; 0.05), lower IDO+ (P \u0026lt; 0.05) and increased natural killer cells (uNK) cell numbers (P \u0026lt; 0.001) in the uterus, as well increased NK cells in the placenta (P \u0026lt; 0.05) than in normal pregnant mic...","internal_url":"https://www.academia.edu/123639714/Impact_of_regulatory_T_cell_therapy_on_immune_cell_composition_and_fetal_survival_rate_in_abortion_prone_mice","translated_internal_url":"","created_at":"2024-09-07T04:34:56.409-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Impact_of_regulatory_T_cell_therapy_on_immune_cell_composition_and_fetal_survival_rate_in_abortion_prone_mice","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":654,"name":"Andrology","url":"https://www.academia.edu/Documents/in/Andrology"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences"},{"id":76061,"name":"Placenta","url":"https://www.academia.edu/Documents/in/Placenta"},{"id":216943,"name":"CD","url":"https://www.academia.edu/Documents/in/CD"},{"id":770944,"name":"Fetus","url":"https://www.academia.edu/Documents/in/Fetus"},{"id":987079,"name":"Uterus","url":"https://www.academia.edu/Documents/in/Uterus"},{"id":3718352,"name":"Adoptive Cell Transfer","url":"https://www.academia.edu/Documents/in/Adoptive_Cell_Transfer"},{"id":3763225,"name":"Medical and Health Sciences","url":"https://www.academia.edu/Documents/in/Medical_and_Health_Sciences"}],"urls":[{"id":44518686,"url":"https://www.publish.csiro.au/RD/fulltext/RD22267"}]}, 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="123639713"><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/123639713/Myeloid_derived_suppressor_cells_MDSCs_depletion_by_cabozantinib_improves_the_efficacy_of_anti_HER2_antibody_based_immunotherapy_in_a_4T1_HER2_murine_breast_cancer_model"><img alt="Research paper thumbnail of Myeloid-derived suppressor cells (MDSCs) depletion by cabozantinib improves the efficacy of anti-HER2 antibody-based immunotherapy in a 4T1-HER2 murine breast cancer model" 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/123639713/Myeloid_derived_suppressor_cells_MDSCs_depletion_by_cabozantinib_improves_the_efficacy_of_anti_HER2_antibody_based_immunotherapy_in_a_4T1_HER2_murine_breast_cancer_model">Myeloid-derived suppressor cells (MDSCs) depletion by cabozantinib improves the efficacy of anti-HER2 antibody-based immunotherapy in a 4T1-HER2 murine breast cancer model</a></div><div class="wp-workCard_item"><span>International Immunopharmacology</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="123639713"><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="123639713"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639713; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639713]").text(description); $(".js-view-count[data-work-id=123639713]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639713; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639713']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639713, 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" } } $('.js-work-strip[data-work-id=123639713]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639713,"title":"Myeloid-derived suppressor cells (MDSCs) depletion by cabozantinib improves the efficacy of anti-HER2 antibody-based immunotherapy in a 4T1-HER2 murine breast cancer model","translated_title":"","metadata":{"publisher":"Elsevier BV","publication_name":"International Immunopharmacology"},"translated_abstract":null,"internal_url":"https://www.academia.edu/123639713/Myeloid_derived_suppressor_cells_MDSCs_depletion_by_cabozantinib_improves_the_efficacy_of_anti_HER2_antibody_based_immunotherapy_in_a_4T1_HER2_murine_breast_cancer_model","translated_internal_url":"","created_at":"2024-09-07T04:34:56.136-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Myeloid_derived_suppressor_cells_MDSCs_depletion_by_cabozantinib_improves_the_efficacy_of_anti_HER2_antibody_based_immunotherapy_in_a_4T1_HER2_murine_breast_cancer_model","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":22255,"name":"Cancer Research","url":"https://www.academia.edu/Documents/in/Cancer_Research"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":26699,"name":"Immunopharmacology","url":"https://www.academia.edu/Documents/in/Immunopharmacology"},{"id":126863,"name":"Immunotherapy","url":"https://www.academia.edu/Documents/in/Immunotherapy"},{"id":1405550,"name":"Cabozantinib","url":"https://www.academia.edu/Documents/in/Cabozantinib"},{"id":3789884,"name":"Pharmacology and pharmaceutical sciences","url":"https://www.academia.edu/Documents/in/Pharmacology_and_pharmaceutical_sciences"}],"urls":[{"id":44518685,"url":"https://api.elsevier.com/content/article/PII:S1567576922009559?httpAccept=text/xml"}]}, 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="123639712"><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/123639712/Expression_of_Human_Placenta_specific_1_PLAC1_in_CHO_K1_Cells"><img alt="Research paper thumbnail of Expression of Human Placenta-specific 1 (PLAC1) in CHO-K1 Cells" class="work-thumbnail" src="https://attachments.academia-assets.com/118024525/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/123639712/Expression_of_Human_Placenta_specific_1_PLAC1_in_CHO_K1_Cells">Expression of Human Placenta-specific 1 (PLAC1) in CHO-K1 Cells</a></div><div class="wp-workCard_item"><span>Avicenna Journal of Medical Biotechnology</span><span>, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background: Placenta-specific 1 (PLAC1), as a new Cancer/Testis Antigen (CTA), is frequently expr...</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">Background: Placenta-specific 1 (PLAC1), as a new Cancer/Testis Antigen (CTA), is frequently expressed in a variety of cancers and localized to cytoplasm and plasma membrane. Surface expression of cancer target antigens is of great importance that enables antibody-mediated cancer immunotherapy. The aim of the current study was to express the intact human PLAC1 protein on plasma membrane of a eukaryotic cell as a model for future anti-PLAC1-based cancer immunotherapy. Methods: In the first approach, entire human PLAC1 gene including its own Signal Peptide (SP) was cloned into pIRES2-EGFP and LeGO-iG2 vectors and expressed in CHO-K1 cells. In the second approach, cytosolic and Signal-Anchor (SA) sequence of Transferrin Receptor Protein 1 (TFR1) were fused to extracellular portion of PLAC1 and expressed as above. Expression of PLAC1 was then assessed using Reverse Transcription Polymerase Chain Reaction (RT-PCR), Western Blot (WB), Immunocytochemistry (ICC), Immunofluorescence (IF) and...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="99da31c0c2264c7e3bb988e4de8b733d" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":118024525,"asset_id":123639712,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/118024525/download_file?st=MTczMjQzOTg0Nyw4LjIyMi4yMDguMTQ2&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="123639712"><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="123639712"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639712; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639712]").text(description); $(".js-view-count[data-work-id=123639712]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639712; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639712']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639712, 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: "99da31c0c2264c7e3bb988e4de8b733d" } } $('.js-work-strip[data-work-id=123639712]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639712,"title":"Expression of Human Placenta-specific 1 (PLAC1) in CHO-K1 Cells","translated_title":"","metadata":{"abstract":"Background: Placenta-specific 1 (PLAC1), as a new Cancer/Testis Antigen (CTA), is frequently expressed in a variety of cancers and localized to cytoplasm and plasma membrane. Surface expression of cancer target antigens is of great importance that enables antibody-mediated cancer immunotherapy. The aim of the current study was to express the intact human PLAC1 protein on plasma membrane of a eukaryotic cell as a model for future anti-PLAC1-based cancer immunotherapy. Methods: In the first approach, entire human PLAC1 gene including its own Signal Peptide (SP) was cloned into pIRES2-EGFP and LeGO-iG2 vectors and expressed in CHO-K1 cells. In the second approach, cytosolic and Signal-Anchor (SA) sequence of Transferrin Receptor Protein 1 (TFR1) were fused to extracellular portion of PLAC1 and expressed as above. Expression of PLAC1 was then assessed using Reverse Transcription Polymerase Chain Reaction (RT-PCR), Western Blot (WB), Immunocytochemistry (ICC), Immunofluorescence (IF) and...","publisher":"Avicenna journal of medical biotechnology","publication_date":{"day":null,"month":null,"year":2020,"errors":{}},"publication_name":"Avicenna Journal of Medical Biotechnology"},"translated_abstract":"Background: Placenta-specific 1 (PLAC1), as a new Cancer/Testis Antigen (CTA), is frequently expressed in a variety of cancers and localized to cytoplasm and plasma membrane. Surface expression of cancer target antigens is of great importance that enables antibody-mediated cancer immunotherapy. The aim of the current study was to express the intact human PLAC1 protein on plasma membrane of a eukaryotic cell as a model for future anti-PLAC1-based cancer immunotherapy. 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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="123639708"><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/123639708/Adoptive_cell_therapy_with_induced_regulatory_T_cells_normalises_the_abortion_rate_in_abortion_prone_mice"><img alt="Research paper thumbnail of Adoptive cell therapy with induced regulatory T cells normalises the abortion rate in abortion-prone mice" 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/123639708/Adoptive_cell_therapy_with_induced_regulatory_T_cells_normalises_the_abortion_rate_in_abortion_prone_mice">Adoptive cell therapy with induced regulatory T cells normalises the abortion rate in abortion-prone mice</a></div><div class="wp-workCard_item"><span>Reproduction, Fertility and Development</span><span>, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Ovarian hormones drive invivo generation of regulatory T cells (Tregs) during pregnancy. Little i...</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">Ovarian hormones drive invivo generation of regulatory T cells (Tregs) during pregnancy. Little is known about the therapeutic potential of invitro hormone-derived Tregs in pregnancy loss. We investigated the effects of hormone-induced Tregs in a murine model of abortion. CD4+CD25- T cells were isolated from the spleens of CBA/J mice and stimulated with either 17β-oestradiol (E2), progesterone (P4) or transforming growth factor-β1 (TGFB1) plus retinoic acid (RA) for 4 days to generate induced Tregs (iTregs). On Days 1-4 of gestation, DBA/2-mated pregnant CBA/J female mice (abortion prone) were injected intravenously with iTregs or Tregs isolated from normal BALB/c-mated pregnant CBA/J mice (np-Tregs). On Day 14, the number of resorbed fetuses was assessed. Serum interferon (IFN)-γ and uterine forkhead box p3 (Foxp3) expression was analysed by ELISA and immunohistochemistry respectively. Using a 3H-thymidine incorporation assay, isolated CD4+CD25+ Tregs induced by the different treatments suppressed the proliferation of CD4+CD25- T cells. Adoptive transfer of iTregs (from all induction groups) significantly decreased fetal resorption in abortion-prone mice. There were no significant changes in serum IFN-γ concentrations after the adoptive transfer of iTregs or np-Tregs. Immunohistochemistry revealed significantly higher Foxp3 expression in gravid uteri from mice injected with np-Tregs and P4-induced iTregs than in the phosphate-buffered saline-treated group. The findings of this study indicate a potential therapeutic benefit of invitro-induced Tregs in patients with recurrent abortion.</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="123639708"><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="123639708"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639708; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639708]").text(description); $(".js-view-count[data-work-id=123639708]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639708; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639708']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639708, 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" } } $('.js-work-strip[data-work-id=123639708]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639708,"title":"Adoptive cell therapy with induced regulatory T cells normalises the abortion rate in abortion-prone mice","translated_title":"","metadata":{"abstract":"Ovarian hormones drive invivo generation of regulatory T cells (Tregs) during pregnancy. Little is known about the therapeutic potential of invitro hormone-derived Tregs in pregnancy loss. We investigated the effects of hormone-induced Tregs in a murine model of abortion. CD4+CD25- T cells were isolated from the spleens of CBA/J mice and stimulated with either 17β-oestradiol (E2), progesterone (P4) or transforming growth factor-β1 (TGFB1) plus retinoic acid (RA) for 4 days to generate induced Tregs (iTregs). On Days 1-4 of gestation, DBA/2-mated pregnant CBA/J female mice (abortion prone) were injected intravenously with iTregs or Tregs isolated from normal BALB/c-mated pregnant CBA/J mice (np-Tregs). On Day 14, the number of resorbed fetuses was assessed. Serum interferon (IFN)-γ and uterine forkhead box p3 (Foxp3) expression was analysed by ELISA and immunohistochemistry respectively. Using a 3H-thymidine incorporation assay, isolated CD4+CD25+ Tregs induced by the different treatments suppressed the proliferation of CD4+CD25- T cells. Adoptive transfer of iTregs (from all induction groups) significantly decreased fetal resorption in abortion-prone mice. There were no significant changes in serum IFN-γ concentrations after the adoptive transfer of iTregs or np-Tregs. Immunohistochemistry revealed significantly higher Foxp3 expression in gravid uteri from mice injected with np-Tregs and P4-induced iTregs than in the phosphate-buffered saline-treated group. The findings of this study indicate a potential therapeutic benefit of invitro-induced Tregs in patients with recurrent abortion.","publisher":"CSIRO Publishing","publication_date":{"day":null,"month":null,"year":2020,"errors":{}},"publication_name":"Reproduction, Fertility and Development"},"translated_abstract":"Ovarian hormones drive invivo generation of regulatory T cells (Tregs) during pregnancy. Little is known about the therapeutic potential of invitro hormone-derived Tregs in pregnancy loss. We investigated the effects of hormone-induced Tregs in a murine model of abortion. CD4+CD25- T cells were isolated from the spleens of CBA/J mice and stimulated with either 17β-oestradiol (E2), progesterone (P4) or transforming growth factor-β1 (TGFB1) plus retinoic acid (RA) for 4 days to generate induced Tregs (iTregs). On Days 1-4 of gestation, DBA/2-mated pregnant CBA/J female mice (abortion prone) were injected intravenously with iTregs or Tregs isolated from normal BALB/c-mated pregnant CBA/J mice (np-Tregs). On Day 14, the number of resorbed fetuses was assessed. Serum interferon (IFN)-γ and uterine forkhead box p3 (Foxp3) expression was analysed by ELISA and immunohistochemistry respectively. Using a 3H-thymidine incorporation assay, isolated CD4+CD25+ Tregs induced by the different treatments suppressed the proliferation of CD4+CD25- T cells. Adoptive transfer of iTregs (from all induction groups) significantly decreased fetal resorption in abortion-prone mice. There were no significant changes in serum IFN-γ concentrations after the adoptive transfer of iTregs or np-Tregs. Immunohistochemistry revealed significantly higher Foxp3 expression in gravid uteri from mice injected with np-Tregs and P4-induced iTregs than in the phosphate-buffered saline-treated group. The findings of this study indicate a potential therapeutic benefit of invitro-induced Tregs in patients with recurrent abortion.","internal_url":"https://www.academia.edu/123639708/Adoptive_cell_therapy_with_induced_regulatory_T_cells_normalises_the_abortion_rate_in_abortion_prone_mice","translated_internal_url":"","created_at":"2024-09-07T04:34:55.207-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Adoptive_cell_therapy_with_induced_regulatory_T_cells_normalises_the_abortion_rate_in_abortion_prone_mice","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"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":29126,"name":"Abortion","url":"https://www.academia.edu/Documents/in/Abortion"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences"},{"id":3718352,"name":"Adoptive Cell Transfer","url":"https://www.academia.edu/Documents/in/Adoptive_Cell_Transfer"},{"id":3763225,"name":"Medical and Health Sciences","url":"https://www.academia.edu/Documents/in/Medical_and_Health_Sciences"}],"urls":[]}, 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="123639707"><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/123639707/Ror1_Targeting_Monoclonal_Antibodies_Induced_Apoptosis_of_Chronic_Lymphocytic_Leukemia_Cells_A_Potential_Novel_Therapeutic_Approach"><img alt="Research paper thumbnail of Ror1 Targeting Monoclonal Antibodies Induced Apoptosis of Chronic Lymphocytic Leukemia Cells– A Potential Novel Therapeutic Approach" 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/123639707/Ror1_Targeting_Monoclonal_Antibodies_Induced_Apoptosis_of_Chronic_Lymphocytic_Leukemia_Cells_A_Potential_Novel_Therapeutic_Approach">Ror1 Targeting Monoclonal Antibodies Induced Apoptosis of Chronic Lymphocytic Leukemia Cells– A Potential Novel Therapeutic Approach</a></div><div class="wp-workCard_item"><span>Blood</span><span>, 2010</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">916 Methods: A peptide-based mouse monoclonal antibody generation method was used for producing M...</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">916 Methods: A peptide-based mouse monoclonal antibody generation method was used for producing MAbs against the three extracellular domains of Ror1. Twenty CLL patients (10 with progressive and 10 with non-progressive disease) were enrolled in this study. Flow cytometry was used for surface staining of Ror1. Annexin V and propidium iodide (flow cytometry) as well as PARP cleavage (Western blot) was used for detection of apoptosis. Results: Six monoclonal antibodies of different isotypes (IgG, IgM) were produced against Ror1. The frequency of Ror1 positive cells were in the range of 24–89%. Patients with progressive disease had a significantly higher number of Ror1 positive cells as compared to those with non-progressive disease as well as in patients with unmutated compared to mutated IgVH genes. All six antibodies alone induced apoptosis (Annexin V and PARP cleavage) of CLL cells. A higher frequency of apoptotic CLL cells was induced by the antibodies against the CRD region (ligan...</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="123639707"><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="123639707"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639707; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639707]").text(description); $(".js-view-count[data-work-id=123639707]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639707; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639707']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639707, 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" } } $('.js-work-strip[data-work-id=123639707]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639707,"title":"Ror1 Targeting Monoclonal Antibodies Induced Apoptosis of Chronic Lymphocytic Leukemia Cells– A Potential Novel Therapeutic Approach","translated_title":"","metadata":{"abstract":"916 Methods: A peptide-based mouse monoclonal antibody generation method was used for producing MAbs against the three extracellular domains of Ror1. Twenty CLL patients (10 with progressive and 10 with non-progressive disease) were enrolled in this study. Flow cytometry was used for surface staining of Ror1. Annexin V and propidium iodide (flow cytometry) as well as PARP cleavage (Western blot) was used for detection of apoptosis. Results: Six monoclonal antibodies of different isotypes (IgG, IgM) were produced against Ror1. The frequency of Ror1 positive cells were in the range of 24–89%. Patients with progressive disease had a significantly higher number of Ror1 positive cells as compared to those with non-progressive disease as well as in patients with unmutated compared to mutated IgVH genes. All six antibodies alone induced apoptosis (Annexin V and PARP cleavage) of CLL cells. A higher frequency of apoptotic CLL cells was induced by the antibodies against the CRD region (ligan...","publisher":"American Society of Hematology","publication_date":{"day":null,"month":null,"year":2010,"errors":{}},"publication_name":"Blood"},"translated_abstract":"916 Methods: A peptide-based mouse monoclonal antibody generation method was used for producing MAbs against the three extracellular domains of Ror1. Twenty CLL patients (10 with progressive and 10 with non-progressive disease) were enrolled in this study. Flow cytometry was used for surface staining of Ror1. Annexin V and propidium iodide (flow cytometry) as well as PARP cleavage (Western blot) was used for detection of apoptosis. Results: Six monoclonal antibodies of different isotypes (IgG, IgM) were produced against Ror1. The frequency of Ror1 positive cells were in the range of 24–89%. Patients with progressive disease had a significantly higher number of Ror1 positive cells as compared to those with non-progressive disease as well as in patients with unmutated compared to mutated IgVH genes. All six antibodies alone induced apoptosis (Annexin V and PARP cleavage) of CLL cells. 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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="123639761"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" rel="nofollow" href="https://www.academia.edu/123639761/Purification_of_inhibin_from_human_follicular_fluid_using_monoclonal_antibody"><img alt="Research paper thumbnail of Purification of inhibin from human follicular fluid using monoclonal antibody" 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" rel="nofollow" href="https://www.academia.edu/123639761/Purification_of_inhibin_from_human_follicular_fluid_using_monoclonal_antibody">Purification of inhibin from human follicular fluid using monoclonal antibody</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">PURIFICATION OF INHIBIN FROM HUMAN FOLLICULAR FLUID USING MONOCLONAL ANTIBODY SADEGHI MR*,HOJAT M...</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">PURIFICATION OF INHIBIN FROM HUMAN FOLLICULAR FLUID USING MONOCLONAL ANTIBODY SADEGHI MR*,HOJAT MAHSHID,NASERI NIMA,JEDI TEHRANI MAHMOUD,MOSAFANARIMAN,AKHOUNDI MOHAMMAD MAHDI,GHODS R.,BAYAT AA * DEPARTMENT OF ...</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="123639761"><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="123639761"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639761; 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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="123639723"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" rel="nofollow" href="https://www.academia.edu/123639723/Comparison_of_different_transient_gene_expression_systems_for_the_production_of_a_new_humanized_anti_HER2_monoclonal_antibody_Hersintuzumab_"><img alt="Research paper thumbnail of Comparison of different transient gene expression systems for the production of a new humanized anti-HER2 monoclonal antibody (Hersintuzumab)" 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" rel="nofollow" href="https://www.academia.edu/123639723/Comparison_of_different_transient_gene_expression_systems_for_the_production_of_a_new_humanized_anti_HER2_monoclonal_antibody_Hersintuzumab_">Comparison of different transient gene expression systems for the production of a new humanized anti-HER2 monoclonal antibody (Hersintuzumab)</a></div><div class="wp-workCard_item"><span>DARU Journal of Pharmaceutical Sciences</span><span>, Sep 10, 2023</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="123639723"><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="123639723"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639723; 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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="123639722"><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/123639722/Expression_Purification_and_Characterization_of_Three_Overlapping_Immunodominant_Recombinant_Fragments_from_Bordetella_pertussis_Filamentous_Hemagglutinin"><img alt="Research paper thumbnail of Expression, Purification and Characterization of Three Overlapping Immunodominant Recombinant Fragments from Bordetella pertussis Filamentous Hemagglutinin" 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/123639722/Expression_Purification_and_Characterization_of_Three_Overlapping_Immunodominant_Recombinant_Fragments_from_Bordetella_pertussis_Filamentous_Hemagglutinin">Expression, Purification and Characterization of Three Overlapping Immunodominant Recombinant Fragments from Bordetella pertussis Filamentous Hemagglutinin</a></div><div class="wp-workCard_item"><span>PubMed</span><span>, 2013</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background: Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigen...</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">Background: Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigens of Bordetella pertussis (B. pertussis) and a major component of the acellular pertussis vaccine. In the present study, three overlapping recombinant fragments from the immunodominant region of FHA were produced and their immunogenicity was investigated. Methods: Three overlapping coding sequences of FHA antigen were amplified from B. pertussis genomic DNA by PCR. Amplified fragments were expressed in Escherichia coli (E. coli) BL21(DE3) strain and purified through His-tag using Nickel-based chromatography. Purified fragments were characterized by SDS-PAGE and Western blotting techniques. In vitro peripheral blood mononuclear cells (PBMC) proliferation and IFN-γ production were assessed in a limited number of healthy adults vaccinated with a commercial acellular pertussis vaccine in response to all purified FHA fragments by H3-Thymidine incorporation and ELISA, respectively. Results: Recombinant FHA segments were successfully cloned and produced at high levels in E. coli BL21(DE3). SDS-PAGE and Western blot analyses confirmed their purity and reactivity. All three recombinant fragments together with a commercial native FHA were able to induce in vitro PBMC proliferation and IFN-γ production. Conclusion: Our preliminary results suggest that these overlapping recombinant FHA fragments are immunogenic and may prove to be immuno-protective.</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="123639722"><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="123639722"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639722; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639722]").text(description); $(".js-view-count[data-work-id=123639722]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639722; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639722']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639722, 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" } } $('.js-work-strip[data-work-id=123639722]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639722,"title":"Expression, Purification and Characterization of Three Overlapping Immunodominant Recombinant Fragments from Bordetella pertussis Filamentous Hemagglutinin","translated_title":"","metadata":{"abstract":"Background: Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigens of Bordetella pertussis (B. pertussis) and a major component of the acellular pertussis vaccine. In the present study, three overlapping recombinant fragments from the immunodominant region of FHA were produced and their immunogenicity was investigated. Methods: Three overlapping coding sequences of FHA antigen were amplified from B. pertussis genomic DNA by PCR. Amplified fragments were expressed in Escherichia coli (E. coli) BL21(DE3) strain and purified through His-tag using Nickel-based chromatography. Purified fragments were characterized by SDS-PAGE and Western blotting techniques. In vitro peripheral blood mononuclear cells (PBMC) proliferation and IFN-γ production were assessed in a limited number of healthy adults vaccinated with a commercial acellular pertussis vaccine in response to all purified FHA fragments by H3-Thymidine incorporation and ELISA, respectively. Results: Recombinant FHA segments were successfully cloned and produced at high levels in E. coli BL21(DE3). SDS-PAGE and Western blot analyses confirmed their purity and reactivity. All three recombinant fragments together with a commercial native FHA were able to induce in vitro PBMC proliferation and IFN-γ production. Conclusion: Our preliminary results suggest that these overlapping recombinant FHA fragments are immunogenic and may prove to be immuno-protective.","publication_date":{"day":null,"month":null,"year":2013,"errors":{}},"publication_name":"PubMed"},"translated_abstract":"Background: Filamentous hemagglutinin (FHA) is one of the most important immunoprotective antigens of Bordetella pertussis (B. pertussis) and a major component of the acellular pertussis vaccine. In the present study, three overlapping recombinant fragments from the immunodominant region of FHA were produced and their immunogenicity was investigated. Methods: Three overlapping coding sequences of FHA antigen were amplified from B. pertussis genomic DNA by PCR. Amplified fragments were expressed in Escherichia coli (E. coli) BL21(DE3) strain and purified through His-tag using Nickel-based chromatography. Purified fragments were characterized by SDS-PAGE and Western blotting techniques. In vitro peripheral blood mononuclear cells (PBMC) proliferation and IFN-γ production were assessed in a limited number of healthy adults vaccinated with a commercial acellular pertussis vaccine in response to all purified FHA fragments by H3-Thymidine incorporation and ELISA, respectively. Results: Recombinant FHA segments were successfully cloned and produced at high levels in E. coli BL21(DE3). SDS-PAGE and Western blot analyses confirmed their purity and reactivity. All three recombinant fragments together with a commercial native FHA were able to induce in vitro PBMC proliferation and IFN-γ production. Conclusion: Our preliminary results suggest that these overlapping recombinant FHA fragments are immunogenic and may prove to be immuno-protective.","internal_url":"https://www.academia.edu/123639722/Expression_Purification_and_Characterization_of_Three_Overlapping_Immunodominant_Recombinant_Fragments_from_Bordetella_pertussis_Filamentous_Hemagglutinin","translated_internal_url":"","created_at":"2024-09-07T04:35:00.228-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Expression_Purification_and_Characterization_of_Three_Overlapping_Immunodominant_Recombinant_Fragments_from_Bordetella_pertussis_Filamentous_Hemagglutinin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":159,"name":"Microbiology","url":"https://www.academia.edu/Documents/in/Microbiology"},{"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":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":98939,"name":"Pubmed","url":"https://www.academia.edu/Documents/in/Pubmed"},{"id":259819,"name":"Recombinant DNA","url":"https://www.academia.edu/Documents/in/Recombinant_DNA"},{"id":1314192,"name":"Immunogenicity","url":"https://www.academia.edu/Documents/in/Immunogenicity"},{"id":1714726,"name":"Bordetella Pertussis","url":"https://www.academia.edu/Documents/in/Bordetella_Pertussis"}],"urls":[{"id":44518695,"url":"https://pubmed.ncbi.nlm.nih.gov/23626873"}]}, 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="123639721"><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/123639721/Production_and_characterization_of_polyclonal_antibody_against_a_synthetic_peptide_from_%CE%B2_actin_protein"><img alt="Research paper thumbnail of Production and characterization of polyclonal antibody against a synthetic peptide from β-actin protein" 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/123639721/Production_and_characterization_of_polyclonal_antibody_against_a_synthetic_peptide_from_%CE%B2_actin_protein">Production and characterization of polyclonal antibody against a synthetic peptide from β-actin protein</a></div><div class="wp-workCard_item"><span>PubMed</span><span>, Jun 1, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Objectives: Antibodies against actin, as one of the most widely studied structural and multifunct...</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">Objectives: Antibodies against actin, as one of the most widely studied structural and multifunctional housekeeping proteins in eukaryotic cells, are used as internal loading controls in western blot analyses. The aim of this study was to produce polyclonal antibody against a synthetic peptide derived from N-terminal region of β-actin protein to be used as a protein loading control in western blot and other assay systems. Materials and methods: A synthetic peptide derived from β-actin protein was designed and conjugated to Keyhole limpet hemocyanin (KLH) and used to immunize a white New Zealand rabbit. The antibody was purified from serum by affinity chromatography column. The purity of the antibody was determined by SDS-PAGE and its ability to recognize the immunizing peptide was measured by ELISA. The reactivity of the antibody with β-actin protein in a panel of different cell lysates was then evaluated by western blot. In addition, the reactivity of the antibody with the corresponding protein was also evaluated by Immunocytochemistry and Immunohistochemistry in different samples. Results: The antibody could recognize the immunizing peptide in ELISA. It could also recognize β-actin protein in western blot as well as in immunocytochemistry and immunohistochemistry. Conclusion: Our data suggest that this antibody may be used as an internal control in western blot analyses as well as in other immunological applications such as ELISA, immunocytochemistry and immunohistochemistry.</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="123639721"><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="123639721"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639721; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639721]").text(description); $(".js-view-count[data-work-id=123639721]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639721; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639721']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639721, 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" } } $('.js-work-strip[data-work-id=123639721]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639721,"title":"Production and characterization of polyclonal antibody against a synthetic peptide from β-actin protein","translated_title":"","metadata":{"abstract":"Objectives: Antibodies against actin, as one of the most widely studied structural and multifunctional housekeeping proteins in eukaryotic cells, are used as internal loading controls in western blot analyses. The aim of this study was to produce polyclonal antibody against a synthetic peptide derived from N-terminal region of β-actin protein to be used as a protein loading control in western blot and other assay systems. Materials and methods: A synthetic peptide derived from β-actin protein was designed and conjugated to Keyhole limpet hemocyanin (KLH) and used to immunize a white New Zealand rabbit. The antibody was purified from serum by affinity chromatography column. The purity of the antibody was determined by SDS-PAGE and its ability to recognize the immunizing peptide was measured by ELISA. The reactivity of the antibody with β-actin protein in a panel of different cell lysates was then evaluated by western blot. In addition, the reactivity of the antibody with the corresponding protein was also evaluated by Immunocytochemistry and Immunohistochemistry in different samples. Results: The antibody could recognize the immunizing peptide in ELISA. It could also recognize β-actin protein in western blot as well as in immunocytochemistry and immunohistochemistry. Conclusion: Our data suggest that this antibody may be used as an internal control in western blot analyses as well as in other immunological applications such as ELISA, immunocytochemistry and immunohistochemistry.","publication_date":{"day":1,"month":6,"year":2014,"errors":{}},"publication_name":"PubMed"},"translated_abstract":"Objectives: Antibodies against actin, as one of the most widely studied structural and multifunctional housekeeping proteins in eukaryotic cells, are used as internal loading controls in western blot analyses. The aim of this study was to produce polyclonal antibody against a synthetic peptide derived from N-terminal region of β-actin protein to be used as a protein loading control in western blot and other assay systems. Materials and methods: A synthetic peptide derived from β-actin protein was designed and conjugated to Keyhole limpet hemocyanin (KLH) and used to immunize a white New Zealand rabbit. The antibody was purified from serum by affinity chromatography column. The purity of the antibody was determined by SDS-PAGE and its ability to recognize the immunizing peptide was measured by ELISA. The reactivity of the antibody with β-actin protein in a panel of different cell lysates was then evaluated by western blot. In addition, the reactivity of the antibody with the corresponding protein was also evaluated by Immunocytochemistry and Immunohistochemistry in different samples. Results: The antibody could recognize the immunizing peptide in ELISA. It could also recognize β-actin protein in western blot as well as in immunocytochemistry and immunohistochemistry. Conclusion: Our data suggest that this antibody may be used as an internal control in western blot analyses as well as in other immunological applications such as ELISA, immunocytochemistry and immunohistochemistry.","internal_url":"https://www.academia.edu/123639721/Production_and_characterization_of_polyclonal_antibody_against_a_synthetic_peptide_from_%CE%B2_actin_protein","translated_internal_url":"","created_at":"2024-09-07T04:35:00.014-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Production_and_characterization_of_polyclonal_antibody_against_a_synthetic_peptide_from_β_actin_protein","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":12071,"name":"Immunohistochemistry","url":"https://www.academia.edu/Documents/in/Immunohistochemistry"},{"id":37895,"name":"Immunocytochemistry","url":"https://www.academia.edu/Documents/in/Immunocytochemistry"},{"id":98939,"name":"Pubmed","url":"https://www.academia.edu/Documents/in/Pubmed"},{"id":201296,"name":"Peptide","url":"https://www.academia.edu/Documents/in/Peptide"},{"id":357811,"name":"Antibody","url":"https://www.academia.edu/Documents/in/Antibody"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":470726,"name":"Polyclonal Antibodies","url":"https://www.academia.edu/Documents/in/Polyclonal_Antibodies"}],"urls":[{"id":44518694,"url":"https://pubmed.ncbi.nlm.nih.gov/25140199"}]}, 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="123639720"><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/123639720/Production_and_characterization_of_a_murine_monoclonal_antibody_against_human_ferritin"><img alt="Research paper thumbnail of Production and characterization of a murine monoclonal antibody against human ferritin" 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/123639720/Production_and_characterization_of_a_murine_monoclonal_antibody_against_human_ferritin">Production and characterization of a murine monoclonal antibody against human ferritin</a></div><div class="wp-workCard_item"><span>PubMed</span><span>, Oct 1, 2013</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background: Ferritin is an iron storage protein, which plays a key role in iron metabolism. Measu...</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">Background: Ferritin is an iron storage protein, which plays a key role in iron metabolism. Measurement of ferritin level in serum is one of the most useful indicators of iron status and also a sensitive measurement of iron deficiency. Monoclonal antibodies may be useful as a tool in various aspects of ferritin investigations. In this paper, the production of a murine monoclonal antibody (mAb) against human ferritin was reported. Methods: Balb/c mice were immunized with purified human ferritin and splenocytes of hyper immunized mice were fused with Sp2/0 myeloma cells. After four times of cloning by limiting dilution, a positive hybridoma (clone: 2F9-C9) was selected by ELISA using human ferritin. Anti-ferritin mAb was purified from culture supernatants by affinity chromatography. Results: Determination of the antibody affinity for ferritin by ELISA revealed a relatively high affinity (2.34×10(9) M (-1)) and the isotype was determined to be IgG2a. The anti-ferritin mAb 2F9-C9 reacted with 79.4% of Hela cells in flow cytometry. The antibody detected a band of 20 kDa in K562 cells, murine and human liver lysates, purified ferritin in Western blot and also ferritin in human serum. Conclusion: This mAb can specifically recognize ferritin and may serve as a component of ferritin diagnostic kit if other requirements of the kit are met.</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="123639720"><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="123639720"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639720; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639720]").text(description); $(".js-view-count[data-work-id=123639720]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639720; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639720']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639720, 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" } } $('.js-work-strip[data-work-id=123639720]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639720,"title":"Production and characterization of a murine monoclonal antibody against human ferritin","translated_title":"","metadata":{"abstract":"Background: Ferritin is an iron storage protein, which plays a key role in iron metabolism. Measurement of ferritin level in serum is one of the most useful indicators of iron status and also a sensitive measurement of iron deficiency. Monoclonal antibodies may be useful as a tool in various aspects of ferritin investigations. In this paper, the production of a murine monoclonal antibody (mAb) against human ferritin was reported. Methods: Balb/c mice were immunized with purified human ferritin and splenocytes of hyper immunized mice were fused with Sp2/0 myeloma cells. After four times of cloning by limiting dilution, a positive hybridoma (clone: 2F9-C9) was selected by ELISA using human ferritin. Anti-ferritin mAb was purified from culture supernatants by affinity chromatography. Results: Determination of the antibody affinity for ferritin by ELISA revealed a relatively high affinity (2.34×10(9) M (-1)) and the isotype was determined to be IgG2a. The anti-ferritin mAb 2F9-C9 reacted with 79.4% of Hela cells in flow cytometry. The antibody detected a band of 20 kDa in K562 cells, murine and human liver lysates, purified ferritin in Western blot and also ferritin in human serum. Conclusion: This mAb can specifically recognize ferritin and may serve as a component of ferritin diagnostic kit if other requirements of the kit are met.","publication_date":{"day":1,"month":10,"year":2013,"errors":{}},"publication_name":"PubMed"},"translated_abstract":"Background: Ferritin is an iron storage protein, which plays a key role in iron metabolism. Measurement of ferritin level in serum is one of the most useful indicators of iron status and also a sensitive measurement of iron deficiency. Monoclonal antibodies may be useful as a tool in various aspects of ferritin investigations. In this paper, the production of a murine monoclonal antibody (mAb) against human ferritin was reported. Methods: Balb/c mice were immunized with purified human ferritin and splenocytes of hyper immunized mice were fused with Sp2/0 myeloma cells. After four times of cloning by limiting dilution, a positive hybridoma (clone: 2F9-C9) was selected by ELISA using human ferritin. Anti-ferritin mAb was purified from culture supernatants by affinity chromatography. Results: Determination of the antibody affinity for ferritin by ELISA revealed a relatively high affinity (2.34×10(9) M (-1)) and the isotype was determined to be IgG2a. The anti-ferritin mAb 2F9-C9 reacted with 79.4% of Hela cells in flow cytometry. The antibody detected a band of 20 kDa in K562 cells, murine and human liver lysates, purified ferritin in Western blot and also ferritin in human serum. Conclusion: This mAb can specifically recognize ferritin and may serve as a component of ferritin diagnostic kit if other requirements of the kit are met.","internal_url":"https://www.academia.edu/123639720/Production_and_characterization_of_a_murine_monoclonal_antibody_against_human_ferritin","translated_internal_url":"","created_at":"2024-09-07T04:34:59.748-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Production_and_characterization_of_a_murine_monoclonal_antibody_against_human_ferritin","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":2513,"name":"Molecular Biology","url":"https://www.academia.edu/Documents/in/Molecular_Biology"},{"id":98939,"name":"Pubmed","url":"https://www.academia.edu/Documents/in/Pubmed"},{"id":201241,"name":"Affinity chromatography","url":"https://www.academia.edu/Documents/in/Affinity_chromatography"},{"id":220230,"name":"Ferritin","url":"https://www.academia.edu/Documents/in/Ferritin"},{"id":357811,"name":"Antibody","url":"https://www.academia.edu/Documents/in/Antibody"},{"id":462111,"name":"Western blot","url":"https://www.academia.edu/Documents/in/Western_blot"},{"id":766014,"name":"Monoclonal Antibody","url":"https://www.academia.edu/Documents/in/Monoclonal_Antibody"}],"urls":[{"id":44518693,"url":"https://pubmed.ncbi.nlm.nih.gov/24285995"}]}, 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="123639718"><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/123639718/Extraction_Purification_and_Characterization_of_Lipopolysaccharide_from_Escherichia_coli_and_Salmonella_typhi"><img alt="Research paper thumbnail of Extraction, Purification and Characterization of Lipopolysaccharide from Escherichia coli and Salmonella typhi" 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/123639718/Extraction_Purification_and_Characterization_of_Lipopolysaccharide_from_Escherichia_coli_and_Salmonella_typhi">Extraction, Purification and Characterization of Lipopolysaccharide from Escherichia coli and Salmonella typhi</a></div><div class="wp-workCard_item"><span>PubMed</span><span>, 2011</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Lipopolysaccharide (LPS) is an important structural component of the outer cell membrane complex ...</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">Lipopolysaccharide (LPS) is an important structural component of the outer cell membrane complex of gram negative microorganisms. Its causative role in gram negative bacteria-induced diseases and broad applications in different kinds of cell stimulation experiments provided a conceptual basis for studies directed at the isolation, purification, and detailed chemical characterization of LPS. The main problem with LPS purification protocols is the contamination of the end product with nucleic acids and proteins in variable proportions which could potentially interfere with downstream applications. In this study, a simple procedure for purification of LPS from Escherichia coli (E.coli) and Salmonella typhi (S.typhi) with high purity and very low contaminating nucleic acids and proteins based on the hot phenol-water extraction protocol has been introduced. The purity of extracted LPS was evaluated by silver and coomassie blue staining of SDS-PAGE gels and HPLC analysis. Limulus Amebocyte Lysate (LAL) coagulation activity and rabbit pyrogen assay were exploited to monitor the functionality of purified LPS. The results showed that DNase and RNase treatment of the sample is essential after the sonication step to eliminate nucleic acid contamination in the LPS fraction. Silver staining demonstrated ladder pattern which is characteristic of LPS. No contaminating protein was found as assessed by coomassie blue staining. HPLC fractionation revealed high degree of purity comparable with commercial LPS. Parenteral administration of purified LPS resulted in substantial increase of rabbits' body temperature (mean: 1.45°C). LAL coagulation assay confirmed the functional activity of the purified LPS. In conclusion, the protocol presented here could be employed for isolation of LPS with high purity and functional activity.</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="123639718"><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="123639718"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639718; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639718]").text(description); $(".js-view-count[data-work-id=123639718]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639718; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639718']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639718, 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" } } $('.js-work-strip[data-work-id=123639718]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639718,"title":"Extraction, Purification and Characterization of Lipopolysaccharide from Escherichia coli and Salmonella typhi","translated_title":"","metadata":{"abstract":"Lipopolysaccharide (LPS) is an important structural component of the outer cell membrane complex of gram negative microorganisms. Its causative role in gram negative bacteria-induced diseases and broad applications in different kinds of cell stimulation experiments provided a conceptual basis for studies directed at the isolation, purification, and detailed chemical characterization of LPS. The main problem with LPS purification protocols is the contamination of the end product with nucleic acids and proteins in variable proportions which could potentially interfere with downstream applications. In this study, a simple procedure for purification of LPS from Escherichia coli (E.coli) and Salmonella typhi (S.typhi) with high purity and very low contaminating nucleic acids and proteins based on the hot phenol-water extraction protocol has been introduced. The purity of extracted LPS was evaluated by silver and coomassie blue staining of SDS-PAGE gels and HPLC analysis. Limulus Amebocyte Lysate (LAL) coagulation activity and rabbit pyrogen assay were exploited to monitor the functionality of purified LPS. The results showed that DNase and RNase treatment of the sample is essential after the sonication step to eliminate nucleic acid contamination in the LPS fraction. Silver staining demonstrated ladder pattern which is characteristic of LPS. No contaminating protein was found as assessed by coomassie blue staining. HPLC fractionation revealed high degree of purity comparable with commercial LPS. Parenteral administration of purified LPS resulted in substantial increase of rabbits' body temperature (mean: 1.45°C). LAL coagulation assay confirmed the functional activity of the purified LPS. In conclusion, the protocol presented here could be employed for isolation of LPS with high purity and functional activity.","publication_date":{"day":null,"month":null,"year":2011,"errors":{}},"publication_name":"PubMed"},"translated_abstract":"Lipopolysaccharide (LPS) is an important structural component of the outer cell membrane complex of gram negative microorganisms. Its causative role in gram negative bacteria-induced diseases and broad applications in different kinds of cell stimulation experiments provided a conceptual basis for studies directed at the isolation, purification, and detailed chemical characterization of LPS. The main problem with LPS purification protocols is the contamination of the end product with nucleic acids and proteins in variable proportions which could potentially interfere with downstream applications. In this study, a simple procedure for purification of LPS from Escherichia coli (E.coli) and Salmonella typhi (S.typhi) with high purity and very low contaminating nucleic acids and proteins based on the hot phenol-water extraction protocol has been introduced. The purity of extracted LPS was evaluated by silver and coomassie blue staining of SDS-PAGE gels and HPLC analysis. Limulus Amebocyte Lysate (LAL) coagulation activity and rabbit pyrogen assay were exploited to monitor the functionality of purified LPS. The results showed that DNase and RNase treatment of the sample is essential after the sonication step to eliminate nucleic acid contamination in the LPS fraction. Silver staining demonstrated ladder pattern which is characteristic of LPS. No contaminating protein was found as assessed by coomassie blue staining. HPLC fractionation revealed high degree of purity comparable with commercial LPS. Parenteral administration of purified LPS resulted in substantial increase of rabbits' body temperature (mean: 1.45°C). LAL coagulation assay confirmed the functional activity of the purified LPS. In conclusion, the protocol presented here could be employed for isolation of LPS with high purity and functional activity.","internal_url":"https://www.academia.edu/123639718/Extraction_Purification_and_Characterization_of_Lipopolysaccharide_from_Escherichia_coli_and_Salmonella_typhi","translated_internal_url":"","created_at":"2024-09-07T04:34:58.638-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Extraction_Purification_and_Characterization_of_Lipopolysaccharide_from_Escherichia_coli_and_Salmonella_typhi","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":48183,"name":"Lipopolysaccharide","url":"https://www.academia.edu/Documents/in/Lipopolysaccharide"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":98939,"name":"Pubmed","url":"https://www.academia.edu/Documents/in/Pubmed"},{"id":1256745,"name":"Lysis","url":"https://www.academia.edu/Documents/in/Lysis"},{"id":1727314,"name":"Nucleic Acid","url":"https://www.academia.edu/Documents/in/Nucleic_Acid"}],"urls":[{"id":44518691,"url":"https://pubmed.ncbi.nlm.nih.gov/23407691"}]}, 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="123639717"><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/123639717/Proteome_Analysis_of_Adult_Acute_Lymphoblastic_Leukemia_by_Two_dimensional_Blue_Native_Sodium_Dodecyl_Sulfate_Gel_Electrophoresis"><img alt="Research paper thumbnail of Proteome Analysis of Adult Acute Lymphoblastic Leukemia by Two-dimensional Blue Native/Sodium Dodecyl Sulfate Gel Electrophoresis" 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/123639717/Proteome_Analysis_of_Adult_Acute_Lymphoblastic_Leukemia_by_Two_dimensional_Blue_Native_Sodium_Dodecyl_Sulfate_Gel_Electrophoresis">Proteome Analysis of Adult Acute Lymphoblastic Leukemia by Two-dimensional Blue Native/Sodium Dodecyl Sulfate Gel Electrophoresis</a></div><div class="wp-workCard_item"><span>Avicenna journal of medical biotechnology</span><span>, Dec 20, 2022</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background:Despite the significant progress in the treatment of Acute Lymphoblastic Leukemia (ALL...</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">Background:Despite the significant progress in the treatment of Acute Lymphoblastic Leukemia (ALL) in children, it still remains as one of the most challenging malignancies in adults. Identification of new biomarkers may improve the management of adult ALL. Proteins expressed on the cell surface can be considered as disease-associated biomarkers with potential for diagnosis and targeted therapies. Thus, membrane proteome studies give essential information about the disease-related biomarkers.Methods:We applied 2-dimensional blue-native SDS-PAGE technique followed by MALDI-TOF/TOF-mass spectrometry to study the cell membrane proteome of peripheral blood mononuclear cells of adult B-ALL patients in comparison to that of the healthy controls.Results:Sixty seven differentially expressed protein spots were detected, among them 52 proteins were found to be up-regulated but the other 15 proteins were down-regulated in B-ALL. Five differentially expressed proteins, involved in energy metabolism pathways, were detected in B-ALL patients compared to the healthy control group.Conclusion:Differentially expressed proteins provide an insight into the molecular biology of B-ALL. Further studies must be done to confirm our data to be considered as potential targets for detection and treatment of B-ALL.</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="123639717"><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="123639717"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639717; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639717]").text(description); $(".js-view-count[data-work-id=123639717]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639717; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639717']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639717, 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" } } $('.js-work-strip[data-work-id=123639717]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639717,"title":"Proteome Analysis of Adult Acute Lymphoblastic Leukemia by Two-dimensional Blue Native/Sodium Dodecyl Sulfate Gel Electrophoresis","translated_title":"","metadata":{"abstract":"Background:Despite the significant progress in the treatment of Acute Lymphoblastic Leukemia (ALL) in children, it still remains as one of the most challenging malignancies in adults. Identification of new biomarkers may improve the management of adult ALL. Proteins expressed on the cell surface can be considered as disease-associated biomarkers with potential for diagnosis and targeted therapies. Thus, membrane proteome studies give essential information about the disease-related biomarkers.Methods:We applied 2-dimensional blue-native SDS-PAGE technique followed by MALDI-TOF/TOF-mass spectrometry to study the cell membrane proteome of peripheral blood mononuclear cells of adult B-ALL patients in comparison to that of the healthy controls.Results:Sixty seven differentially expressed protein spots were detected, among them 52 proteins were found to be up-regulated but the other 15 proteins were down-regulated in B-ALL. Five differentially expressed proteins, involved in energy metabolism pathways, were detected in B-ALL patients compared to the healthy control group.Conclusion:Differentially expressed proteins provide an insight into the molecular biology of B-ALL. Further studies must be done to confirm our data to be considered as potential targets for detection and treatment of B-ALL.","publisher":"Knowledge E","publication_date":{"day":20,"month":12,"year":2022,"errors":{}},"publication_name":"Avicenna journal of medical biotechnology"},"translated_abstract":"Background:Despite the significant progress in the treatment of Acute Lymphoblastic Leukemia (ALL) in children, it still remains as one of the most challenging malignancies in adults. Identification of new biomarkers may improve the management of adult ALL. Proteins expressed on the cell surface can be considered as disease-associated biomarkers with potential for diagnosis and targeted therapies. Thus, membrane proteome studies give essential information about the disease-related biomarkers.Methods:We applied 2-dimensional blue-native SDS-PAGE technique followed by MALDI-TOF/TOF-mass spectrometry to study the cell membrane proteome of peripheral blood mononuclear cells of adult B-ALL patients in comparison to that of the healthy controls.Results:Sixty seven differentially expressed protein spots were detected, among them 52 proteins were found to be up-regulated but the other 15 proteins were down-regulated in B-ALL. Five differentially expressed proteins, involved in energy metabolism pathways, were detected in B-ALL patients compared to the healthy control group.Conclusion:Differentially expressed proteins provide an insight into the molecular biology of B-ALL. Further studies must be done to confirm our data to be considered as potential targets for detection and treatment of B-ALL.","internal_url":"https://www.academia.edu/123639717/Proteome_Analysis_of_Adult_Acute_Lymphoblastic_Leukemia_by_Two_dimensional_Blue_Native_Sodium_Dodecyl_Sulfate_Gel_Electrophoresis","translated_internal_url":"","created_at":"2024-09-07T04:34:57.195-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Proteome_Analysis_of_Adult_Acute_Lymphoblastic_Leukemia_by_Two_dimensional_Blue_Native_Sodium_Dodecyl_Sulfate_Gel_Electrophoresis","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":759403,"name":"Gel electrophoresis","url":"https://www.academia.edu/Documents/in/Gel_electrophoresis"},{"id":1035050,"name":"Proteome","url":"https://www.academia.edu/Documents/in/Proteome"},{"id":2622517,"name":"Sodium Dodecyl Sulfate","url":"https://www.academia.edu/Documents/in/Sodium_Dodecyl_Sulfate"}],"urls":[{"id":44518690,"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9895978"}]}, 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="123639716"><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/123639716/Cloning_Expression_and_Characterization_of_a_Peptibody_To_Deplete_Myeloid_Derived_Suppressor_Cells_in_a_Murine_Mammary_Carcinoma_Model"><img alt="Research paper thumbnail of Cloning, Expression and Characterization of a Peptibody To Deplete Myeloid Derived Suppressor Cells in a Murine Mammary Carcinoma Model" class="work-thumbnail" src="https://attachments.academia-assets.com/118024543/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/123639716/Cloning_Expression_and_Characterization_of_a_Peptibody_To_Deplete_Myeloid_Derived_Suppressor_Cells_in_a_Murine_Mammary_Carcinoma_Model">Cloning, Expression and Characterization of a Peptibody To Deplete Myeloid Derived Suppressor Cells in a Murine Mammary Carcinoma Model</a></div><div class="wp-workCard_item"><span>Research Square (Research Square)</span><span>, Dec 28, 2021</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="5df65146b38fa450fb7bd4f07c88615f" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":118024543,"asset_id":123639716,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/118024543/download_file?st=MTczMjQzOTg0Nyw4LjIyMi4yMDguMTQ2&st=MTczMjQzOTg0Nyw4LjIyMi4yMDguMTQ2&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="123639716"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa 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$('.js-work-strip[data-work-id=123639716]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639716,"title":"Cloning, Expression and Characterization of a Peptibody To Deplete Myeloid Derived Suppressor Cells in a Murine Mammary Carcinoma Model","translated_title":"","metadata":{"publisher":"Research Square","publication_date":{"day":28,"month":12,"year":2021,"errors":{}},"publication_name":"Research Square (Research 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href="https://www.academia.edu/123639715/Immunogenicity_and_reactogenicity_of_two_diphtheria_tetanus_whole_cell_pertussis_vaccines_in_Iranian_pre_school_children_a_randomized_controlled_trial"><img alt="Research paper thumbnail of Immunogenicity and reactogenicity of two diphtheria-tetanus-whole cell pertussis vaccines in Iranian pre-school children, a randomized controlled trial" class="work-thumbnail" src="https://attachments.academia-assets.com/118024528/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/123639715/Immunogenicity_and_reactogenicity_of_two_diphtheria_tetanus_whole_cell_pertussis_vaccines_in_Iranian_pre_school_children_a_randomized_controlled_trial">Immunogenicity and reactogenicity of two diphtheria-tetanus-whole cell pertussis vaccines in Iranian pre-school children, a randomized controlled trial</a></div><div class="wp-workCard_item"><span>Human Vaccines & Immunotherapeutics</span><span>, Jun 12, 2013</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="9c130c498e561c651c2a89ff2f332560" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":118024528,"asset_id":123639715,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/118024528/download_file?st=MTczMjQzOTg0Nyw4LjIyMi4yMDguMTQ2&st=MTczMjQzOTg0Nyw4LjIyMi4yMDguMTQ2&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="123639715"><a class="js-profile-work-strip-edit-button" 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Vaccines","url":"https://www.academia.edu/Documents/in/Hepatitis_B_Vaccines"},{"id":1817270,"name":"Diphtheria","url":"https://www.academia.edu/Documents/in/Diphtheria"},{"id":1990998,"name":"Haemophilus influenzae","url":"https://www.academia.edu/Documents/in/Haemophilus_influenzae"},{"id":2489700,"name":"Child preschool","url":"https://www.academia.edu/Documents/in/Child_preschool"}],"urls":[{"id":44518687,"url":"https://www.tandfonline.com/doi/pdf/10.4161/hv.24093?needAccess=true"}]}, 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="123639714"><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/123639714/Impact_of_regulatory_T_cell_therapy_on_immune_cell_composition_and_fetal_survival_rate_in_abortion_prone_mice"><img alt="Research paper thumbnail of Impact of regulatory T cell therapy on immune cell composition and fetal survival rate in abortion prone mice" 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/123639714/Impact_of_regulatory_T_cell_therapy_on_immune_cell_composition_and_fetal_survival_rate_in_abortion_prone_mice">Impact of regulatory T cell therapy on immune cell composition and fetal survival rate in abortion prone mice</a></div><div class="wp-workCard_item"><span>Reproduction, Fertility and Development</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Context Implantation of fertilised eggs and survival of a semi-allogenic embryo rely on the inter...</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">Context Implantation of fertilised eggs and survival of a semi-allogenic embryo rely on the interactions between the cells and molecules preparing the uterus. We investigated the effect of regulatory T cell (Treg) therapy on the mechanism of local immune tolerance of mice prone to spontaneous abortion. Methods Naive T cells were stimulated in vitro with 17β-oestradiol (E2), progesterone (P4) and TGF-β1 for 96 h to generate induced Tregs (iTreg). The iTregs were injected into DBA/2-mated pregnant CBA/J female mice (abortion prone model). On day 14 of pregnancy, mice were killed and decidual and placental tissues were collected for cellular composition analysis. Results Abortion prone mice (PBS treated) showed significantly lower survival rates (P &lt; 0.0001), increased CD3+CD8+ (P &lt; 0.05), lower IDO+ (P &lt; 0.05) and increased natural killer cells (uNK) cell numbers (P &lt; 0.001) in the uterus, as well increased NK cells in the placenta (P &lt; 0.05) than in normal pregnant mic...</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="123639714"><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="123639714"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639714; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639714]").text(description); $(".js-view-count[data-work-id=123639714]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639714; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639714']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639714, 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" } } $('.js-work-strip[data-work-id=123639714]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639714,"title":"Impact of regulatory T cell therapy on immune cell composition and fetal survival rate in abortion prone mice","translated_title":"","metadata":{"abstract":"Context Implantation of fertilised eggs and survival of a semi-allogenic embryo rely on the interactions between the cells and molecules preparing the uterus. We investigated the effect of regulatory T cell (Treg) therapy on the mechanism of local immune tolerance of mice prone to spontaneous abortion. Methods Naive T cells were stimulated in vitro with 17β-oestradiol (E2), progesterone (P4) and TGF-β1 for 96 h to generate induced Tregs (iTreg). The iTregs were injected into DBA/2-mated pregnant CBA/J female mice (abortion prone model). On day 14 of pregnancy, mice were killed and decidual and placental tissues were collected for cellular composition analysis. Results Abortion prone mice (PBS treated) showed significantly lower survival rates (P \u0026lt; 0.0001), increased CD3+CD8+ (P \u0026lt; 0.05), lower IDO+ (P \u0026lt; 0.05) and increased natural killer cells (uNK) cell numbers (P \u0026lt; 0.001) in the uterus, as well increased NK cells in the placenta (P \u0026lt; 0.05) than in normal pregnant mic...","publisher":"CSIRO Publishing","publication_name":"Reproduction, Fertility and Development"},"translated_abstract":"Context Implantation of fertilised eggs and survival of a semi-allogenic embryo rely on the interactions between the cells and molecules preparing the uterus. We investigated the effect of regulatory T cell (Treg) therapy on the mechanism of local immune tolerance of mice prone to spontaneous abortion. Methods Naive T cells were stimulated in vitro with 17β-oestradiol (E2), progesterone (P4) and TGF-β1 for 96 h to generate induced Tregs (iTreg). The iTregs were injected into DBA/2-mated pregnant CBA/J female mice (abortion prone model). On day 14 of pregnancy, mice were killed and decidual and placental tissues were collected for cellular composition analysis. Results Abortion prone mice (PBS treated) showed significantly lower survival rates (P \u0026lt; 0.0001), increased CD3+CD8+ (P \u0026lt; 0.05), lower IDO+ (P \u0026lt; 0.05) and increased natural killer cells (uNK) cell numbers (P \u0026lt; 0.001) in the uterus, as well increased NK cells in the placenta (P \u0026lt; 0.05) than in normal pregnant mic...","internal_url":"https://www.academia.edu/123639714/Impact_of_regulatory_T_cell_therapy_on_immune_cell_composition_and_fetal_survival_rate_in_abortion_prone_mice","translated_internal_url":"","created_at":"2024-09-07T04:34:56.409-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Impact_of_regulatory_T_cell_therapy_on_immune_cell_composition_and_fetal_survival_rate_in_abortion_prone_mice","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":654,"name":"Andrology","url":"https://www.academia.edu/Documents/in/Andrology"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences"},{"id":76061,"name":"Placenta","url":"https://www.academia.edu/Documents/in/Placenta"},{"id":216943,"name":"CD","url":"https://www.academia.edu/Documents/in/CD"},{"id":770944,"name":"Fetus","url":"https://www.academia.edu/Documents/in/Fetus"},{"id":987079,"name":"Uterus","url":"https://www.academia.edu/Documents/in/Uterus"},{"id":3718352,"name":"Adoptive Cell Transfer","url":"https://www.academia.edu/Documents/in/Adoptive_Cell_Transfer"},{"id":3763225,"name":"Medical and Health Sciences","url":"https://www.academia.edu/Documents/in/Medical_and_Health_Sciences"}],"urls":[{"id":44518686,"url":"https://www.publish.csiro.au/RD/fulltext/RD22267"}]}, 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="123639713"><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/123639713/Myeloid_derived_suppressor_cells_MDSCs_depletion_by_cabozantinib_improves_the_efficacy_of_anti_HER2_antibody_based_immunotherapy_in_a_4T1_HER2_murine_breast_cancer_model"><img alt="Research paper thumbnail of Myeloid-derived suppressor cells (MDSCs) depletion by cabozantinib improves the efficacy of anti-HER2 antibody-based immunotherapy in a 4T1-HER2 murine breast cancer model" 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/123639713/Myeloid_derived_suppressor_cells_MDSCs_depletion_by_cabozantinib_improves_the_efficacy_of_anti_HER2_antibody_based_immunotherapy_in_a_4T1_HER2_murine_breast_cancer_model">Myeloid-derived suppressor cells (MDSCs) depletion by cabozantinib improves the efficacy of anti-HER2 antibody-based immunotherapy in a 4T1-HER2 murine breast cancer model</a></div><div class="wp-workCard_item"><span>International Immunopharmacology</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="123639713"><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="123639713"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639713; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639713]").text(description); $(".js-view-count[data-work-id=123639713]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639713; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639713']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639713, 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" } } $('.js-work-strip[data-work-id=123639713]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639713,"title":"Myeloid-derived suppressor cells (MDSCs) depletion by cabozantinib improves the efficacy of anti-HER2 antibody-based immunotherapy in a 4T1-HER2 murine breast cancer model","translated_title":"","metadata":{"publisher":"Elsevier BV","publication_name":"International Immunopharmacology"},"translated_abstract":null,"internal_url":"https://www.academia.edu/123639713/Myeloid_derived_suppressor_cells_MDSCs_depletion_by_cabozantinib_improves_the_efficacy_of_anti_HER2_antibody_based_immunotherapy_in_a_4T1_HER2_murine_breast_cancer_model","translated_internal_url":"","created_at":"2024-09-07T04:34:56.136-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Myeloid_derived_suppressor_cells_MDSCs_depletion_by_cabozantinib_improves_the_efficacy_of_anti_HER2_antibody_based_immunotherapy_in_a_4T1_HER2_murine_breast_cancer_model","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"id":22255,"name":"Cancer Research","url":"https://www.academia.edu/Documents/in/Cancer_Research"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":26699,"name":"Immunopharmacology","url":"https://www.academia.edu/Documents/in/Immunopharmacology"},{"id":126863,"name":"Immunotherapy","url":"https://www.academia.edu/Documents/in/Immunotherapy"},{"id":1405550,"name":"Cabozantinib","url":"https://www.academia.edu/Documents/in/Cabozantinib"},{"id":3789884,"name":"Pharmacology and pharmaceutical sciences","url":"https://www.academia.edu/Documents/in/Pharmacology_and_pharmaceutical_sciences"}],"urls":[{"id":44518685,"url":"https://api.elsevier.com/content/article/PII:S1567576922009559?httpAccept=text/xml"}]}, 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="123639712"><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/123639712/Expression_of_Human_Placenta_specific_1_PLAC1_in_CHO_K1_Cells"><img alt="Research paper thumbnail of Expression of Human Placenta-specific 1 (PLAC1) in CHO-K1 Cells" class="work-thumbnail" src="https://attachments.academia-assets.com/118024525/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/123639712/Expression_of_Human_Placenta_specific_1_PLAC1_in_CHO_K1_Cells">Expression of Human Placenta-specific 1 (PLAC1) in CHO-K1 Cells</a></div><div class="wp-workCard_item"><span>Avicenna Journal of Medical Biotechnology</span><span>, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background: Placenta-specific 1 (PLAC1), as a new Cancer/Testis Antigen (CTA), is frequently expr...</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">Background: Placenta-specific 1 (PLAC1), as a new Cancer/Testis Antigen (CTA), is frequently expressed in a variety of cancers and localized to cytoplasm and plasma membrane. Surface expression of cancer target antigens is of great importance that enables antibody-mediated cancer immunotherapy. The aim of the current study was to express the intact human PLAC1 protein on plasma membrane of a eukaryotic cell as a model for future anti-PLAC1-based cancer immunotherapy. Methods: In the first approach, entire human PLAC1 gene including its own Signal Peptide (SP) was cloned into pIRES2-EGFP and LeGO-iG2 vectors and expressed in CHO-K1 cells. In the second approach, cytosolic and Signal-Anchor (SA) sequence of Transferrin Receptor Protein 1 (TFR1) were fused to extracellular portion of PLAC1 and expressed as above. Expression of PLAC1 was then assessed using Reverse Transcription Polymerase Chain Reaction (RT-PCR), Western Blot (WB), Immunocytochemistry (ICC), Immunofluorescence (IF) and...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="99da31c0c2264c7e3bb988e4de8b733d" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":118024525,"asset_id":123639712,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/118024525/download_file?st=MTczMjQzOTg0Nyw4LjIyMi4yMDguMTQ2&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="123639712"><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="123639712"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639712; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639712]").text(description); $(".js-view-count[data-work-id=123639712]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639712; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639712']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639712, 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: "99da31c0c2264c7e3bb988e4de8b733d" } } $('.js-work-strip[data-work-id=123639712]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639712,"title":"Expression of Human Placenta-specific 1 (PLAC1) in CHO-K1 Cells","translated_title":"","metadata":{"abstract":"Background: Placenta-specific 1 (PLAC1), as a new Cancer/Testis Antigen (CTA), is frequently expressed in a variety of cancers and localized to cytoplasm and plasma membrane. Surface expression of cancer target antigens is of great importance that enables antibody-mediated cancer immunotherapy. The aim of the current study was to express the intact human PLAC1 protein on plasma membrane of a eukaryotic cell as a model for future anti-PLAC1-based cancer immunotherapy. Methods: In the first approach, entire human PLAC1 gene including its own Signal Peptide (SP) was cloned into pIRES2-EGFP and LeGO-iG2 vectors and expressed in CHO-K1 cells. In the second approach, cytosolic and Signal-Anchor (SA) sequence of Transferrin Receptor Protein 1 (TFR1) were fused to extracellular portion of PLAC1 and expressed as above. Expression of PLAC1 was then assessed using Reverse Transcription Polymerase Chain Reaction (RT-PCR), Western Blot (WB), Immunocytochemistry (ICC), Immunofluorescence (IF) and...","publisher":"Avicenna journal of medical biotechnology","publication_date":{"day":null,"month":null,"year":2020,"errors":{}},"publication_name":"Avicenna Journal of Medical Biotechnology"},"translated_abstract":"Background: Placenta-specific 1 (PLAC1), as a new Cancer/Testis Antigen (CTA), is frequently expressed in a variety of cancers and localized to cytoplasm and plasma membrane. Surface expression of cancer target antigens is of great importance that enables antibody-mediated cancer immunotherapy. The aim of the current study was to express the intact human PLAC1 protein on plasma membrane of a eukaryotic cell as a model for future anti-PLAC1-based cancer immunotherapy. 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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="123639708"><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/123639708/Adoptive_cell_therapy_with_induced_regulatory_T_cells_normalises_the_abortion_rate_in_abortion_prone_mice"><img alt="Research paper thumbnail of Adoptive cell therapy with induced regulatory T cells normalises the abortion rate in abortion-prone mice" 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/123639708/Adoptive_cell_therapy_with_induced_regulatory_T_cells_normalises_the_abortion_rate_in_abortion_prone_mice">Adoptive cell therapy with induced regulatory T cells normalises the abortion rate in abortion-prone mice</a></div><div class="wp-workCard_item"><span>Reproduction, Fertility and Development</span><span>, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Ovarian hormones drive invivo generation of regulatory T cells (Tregs) during pregnancy. Little i...</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">Ovarian hormones drive invivo generation of regulatory T cells (Tregs) during pregnancy. Little is known about the therapeutic potential of invitro hormone-derived Tregs in pregnancy loss. We investigated the effects of hormone-induced Tregs in a murine model of abortion. CD4+CD25- T cells were isolated from the spleens of CBA/J mice and stimulated with either 17β-oestradiol (E2), progesterone (P4) or transforming growth factor-β1 (TGFB1) plus retinoic acid (RA) for 4 days to generate induced Tregs (iTregs). On Days 1-4 of gestation, DBA/2-mated pregnant CBA/J female mice (abortion prone) were injected intravenously with iTregs or Tregs isolated from normal BALB/c-mated pregnant CBA/J mice (np-Tregs). On Day 14, the number of resorbed fetuses was assessed. Serum interferon (IFN)-γ and uterine forkhead box p3 (Foxp3) expression was analysed by ELISA and immunohistochemistry respectively. Using a 3H-thymidine incorporation assay, isolated CD4+CD25+ Tregs induced by the different treatments suppressed the proliferation of CD4+CD25- T cells. Adoptive transfer of iTregs (from all induction groups) significantly decreased fetal resorption in abortion-prone mice. There were no significant changes in serum IFN-γ concentrations after the adoptive transfer of iTregs or np-Tregs. Immunohistochemistry revealed significantly higher Foxp3 expression in gravid uteri from mice injected with np-Tregs and P4-induced iTregs than in the phosphate-buffered saline-treated group. The findings of this study indicate a potential therapeutic benefit of invitro-induced Tregs in patients with recurrent abortion.</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="123639708"><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="123639708"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639708; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639708]").text(description); $(".js-view-count[data-work-id=123639708]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639708; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639708']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639708, 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" } } $('.js-work-strip[data-work-id=123639708]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639708,"title":"Adoptive cell therapy with induced regulatory T cells normalises the abortion rate in abortion-prone mice","translated_title":"","metadata":{"abstract":"Ovarian hormones drive invivo generation of regulatory T cells (Tregs) during pregnancy. Little is known about the therapeutic potential of invitro hormone-derived Tregs in pregnancy loss. We investigated the effects of hormone-induced Tregs in a murine model of abortion. CD4+CD25- T cells were isolated from the spleens of CBA/J mice and stimulated with either 17β-oestradiol (E2), progesterone (P4) or transforming growth factor-β1 (TGFB1) plus retinoic acid (RA) for 4 days to generate induced Tregs (iTregs). On Days 1-4 of gestation, DBA/2-mated pregnant CBA/J female mice (abortion prone) were injected intravenously with iTregs or Tregs isolated from normal BALB/c-mated pregnant CBA/J mice (np-Tregs). On Day 14, the number of resorbed fetuses was assessed. Serum interferon (IFN)-γ and uterine forkhead box p3 (Foxp3) expression was analysed by ELISA and immunohistochemistry respectively. Using a 3H-thymidine incorporation assay, isolated CD4+CD25+ Tregs induced by the different treatments suppressed the proliferation of CD4+CD25- T cells. Adoptive transfer of iTregs (from all induction groups) significantly decreased fetal resorption in abortion-prone mice. There were no significant changes in serum IFN-γ concentrations after the adoptive transfer of iTregs or np-Tregs. Immunohistochemistry revealed significantly higher Foxp3 expression in gravid uteri from mice injected with np-Tregs and P4-induced iTregs than in the phosphate-buffered saline-treated group. The findings of this study indicate a potential therapeutic benefit of invitro-induced Tregs in patients with recurrent abortion.","publisher":"CSIRO Publishing","publication_date":{"day":null,"month":null,"year":2020,"errors":{}},"publication_name":"Reproduction, Fertility and Development"},"translated_abstract":"Ovarian hormones drive invivo generation of regulatory T cells (Tregs) during pregnancy. Little is known about the therapeutic potential of invitro hormone-derived Tregs in pregnancy loss. We investigated the effects of hormone-induced Tregs in a murine model of abortion. CD4+CD25- T cells were isolated from the spleens of CBA/J mice and stimulated with either 17β-oestradiol (E2), progesterone (P4) or transforming growth factor-β1 (TGFB1) plus retinoic acid (RA) for 4 days to generate induced Tregs (iTregs). On Days 1-4 of gestation, DBA/2-mated pregnant CBA/J female mice (abortion prone) were injected intravenously with iTregs or Tregs isolated from normal BALB/c-mated pregnant CBA/J mice (np-Tregs). On Day 14, the number of resorbed fetuses was assessed. Serum interferon (IFN)-γ and uterine forkhead box p3 (Foxp3) expression was analysed by ELISA and immunohistochemistry respectively. Using a 3H-thymidine incorporation assay, isolated CD4+CD25+ Tregs induced by the different treatments suppressed the proliferation of CD4+CD25- T cells. Adoptive transfer of iTregs (from all induction groups) significantly decreased fetal resorption in abortion-prone mice. There were no significant changes in serum IFN-γ concentrations after the adoptive transfer of iTregs or np-Tregs. Immunohistochemistry revealed significantly higher Foxp3 expression in gravid uteri from mice injected with np-Tregs and P4-induced iTregs than in the phosphate-buffered saline-treated group. The findings of this study indicate a potential therapeutic benefit of invitro-induced Tregs in patients with recurrent abortion.","internal_url":"https://www.academia.edu/123639708/Adoptive_cell_therapy_with_induced_regulatory_T_cells_normalises_the_abortion_rate_in_abortion_prone_mice","translated_internal_url":"","created_at":"2024-09-07T04:34:55.207-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Adoptive_cell_therapy_with_induced_regulatory_T_cells_normalises_the_abortion_rate_in_abortion_prone_mice","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"research_interests":[{"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":29126,"name":"Abortion","url":"https://www.academia.edu/Documents/in/Abortion"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences"},{"id":3718352,"name":"Adoptive Cell Transfer","url":"https://www.academia.edu/Documents/in/Adoptive_Cell_Transfer"},{"id":3763225,"name":"Medical and Health Sciences","url":"https://www.academia.edu/Documents/in/Medical_and_Health_Sciences"}],"urls":[]}, 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="123639707"><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/123639707/Ror1_Targeting_Monoclonal_Antibodies_Induced_Apoptosis_of_Chronic_Lymphocytic_Leukemia_Cells_A_Potential_Novel_Therapeutic_Approach"><img alt="Research paper thumbnail of Ror1 Targeting Monoclonal Antibodies Induced Apoptosis of Chronic Lymphocytic Leukemia Cells– A Potential Novel Therapeutic Approach" 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/123639707/Ror1_Targeting_Monoclonal_Antibodies_Induced_Apoptosis_of_Chronic_Lymphocytic_Leukemia_Cells_A_Potential_Novel_Therapeutic_Approach">Ror1 Targeting Monoclonal Antibodies Induced Apoptosis of Chronic Lymphocytic Leukemia Cells– A Potential Novel Therapeutic Approach</a></div><div class="wp-workCard_item"><span>Blood</span><span>, 2010</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">916 Methods: A peptide-based mouse monoclonal antibody generation method was used for producing M...</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">916 Methods: A peptide-based mouse monoclonal antibody generation method was used for producing MAbs against the three extracellular domains of Ror1. Twenty CLL patients (10 with progressive and 10 with non-progressive disease) were enrolled in this study. Flow cytometry was used for surface staining of Ror1. Annexin V and propidium iodide (flow cytometry) as well as PARP cleavage (Western blot) was used for detection of apoptosis. Results: Six monoclonal antibodies of different isotypes (IgG, IgM) were produced against Ror1. The frequency of Ror1 positive cells were in the range of 24–89%. Patients with progressive disease had a significantly higher number of Ror1 positive cells as compared to those with non-progressive disease as well as in patients with unmutated compared to mutated IgVH genes. All six antibodies alone induced apoptosis (Annexin V and PARP cleavage) of CLL cells. A higher frequency of apoptotic CLL cells was induced by the antibodies against the CRD region (ligan...</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="123639707"><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="123639707"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 123639707; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=123639707]").text(description); $(".js-view-count[data-work-id=123639707]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 123639707; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='123639707']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 123639707, 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" } } $('.js-work-strip[data-work-id=123639707]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":123639707,"title":"Ror1 Targeting Monoclonal Antibodies Induced Apoptosis of Chronic Lymphocytic Leukemia Cells– A Potential Novel Therapeutic Approach","translated_title":"","metadata":{"abstract":"916 Methods: A peptide-based mouse monoclonal antibody generation method was used for producing MAbs against the three extracellular domains of Ror1. Twenty CLL patients (10 with progressive and 10 with non-progressive disease) were enrolled in this study. Flow cytometry was used for surface staining of Ror1. Annexin V and propidium iodide (flow cytometry) as well as PARP cleavage (Western blot) was used for detection of apoptosis. Results: Six monoclonal antibodies of different isotypes (IgG, IgM) were produced against Ror1. The frequency of Ror1 positive cells were in the range of 24–89%. Patients with progressive disease had a significantly higher number of Ror1 positive cells as compared to those with non-progressive disease as well as in patients with unmutated compared to mutated IgVH genes. All six antibodies alone induced apoptosis (Annexin V and PARP cleavage) of CLL cells. A higher frequency of apoptotic CLL cells was induced by the antibodies against the CRD region (ligan...","publisher":"American Society of Hematology","publication_date":{"day":null,"month":null,"year":2010,"errors":{}},"publication_name":"Blood"},"translated_abstract":"916 Methods: A peptide-based mouse monoclonal antibody generation method was used for producing MAbs against the three extracellular domains of Ror1. Twenty CLL patients (10 with progressive and 10 with non-progressive disease) were enrolled in this study. Flow cytometry was used for surface staining of Ror1. Annexin V and propidium iodide (flow cytometry) as well as PARP cleavage (Western blot) was used for detection of apoptosis. Results: Six monoclonal antibodies of different isotypes (IgG, IgM) were produced against Ror1. The frequency of Ror1 positive cells were in the range of 24–89%. Patients with progressive disease had a significantly higher number of Ror1 positive cells as compared to those with non-progressive disease as well as in patients with unmutated compared to mutated IgVH genes. All six antibodies alone induced apoptosis (Annexin V and PARP cleavage) of CLL cells. A higher frequency of apoptotic CLL cells was induced by the antibodies against the CRD region (ligan...","internal_url":"https://www.academia.edu/123639707/Ror1_Targeting_Monoclonal_Antibodies_Induced_Apoptosis_of_Chronic_Lymphocytic_Leukemia_Cells_A_Potential_Novel_Therapeutic_Approach","translated_internal_url":"","created_at":"2024-09-07T04:34:54.935-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":50682354,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Ror1_Targeting_Monoclonal_Antibodies_Induced_Apoptosis_of_Chronic_Lymphocytic_Leukemia_Cells_A_Potential_Novel_Therapeutic_Approach","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":50682354,"first_name":"Mahmood","middle_initials":null,"last_name":"Jeddi-tehrani","page_name":"MahmoodJedditehrani","domain_name":"independent","created_at":"2016-07-02T23:59:47.211-07:00","display_name":"Mahmood Jeddi-tehrani","url":"https://independent.academia.edu/MahmoodJedditehrani"},"attachments":[],"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":24731,"name":"Apoptosis","url":"https://www.academia.edu/Documents/in/Apoptosis"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":82976,"name":"Chronic Lymphocytic Leukemia","url":"https://www.academia.edu/Documents/in/Chronic_Lymphocytic_Leukemia"},{"id":100732,"name":"Blood","url":"https://www.academia.edu/Documents/in/Blood"},{"id":244814,"name":"Clinical Sciences","url":"https://www.academia.edu/Documents/in/Clinical_Sciences"},{"id":357811,"name":"Antibody","url":"https://www.academia.edu/Documents/in/Antibody"},{"id":766014,"name":"Monoclonal Antibody","url":"https://www.academia.edu/Documents/in/Monoclonal_Antibody"},{"id":1335154,"name":"Propidium Iodide","url":"https://www.academia.edu/Documents/in/Propidium_Iodide"},{"id":3101476,"name":"Annexin","url":"https://www.academia.edu/Documents/in/Annexin"},{"id":3789879,"name":"Cardiovascular medicine and haematology","url":"https://www.academia.edu/Documents/in/Cardiovascular_medicine_and_haematology"},{"id":3789883,"name":"Paediatrics and reproductive medicine","url":"https://www.academia.edu/Documents/in/Paediatrics_and_reproductive_medicine"}],"urls":[{"id":44518682,"url":"https://ashpublications.org/blood/article/116/21/916/70153/Ror1-Targeting-Monoclonal-Antibodies-Induced"}]}, dispatcherData: dispatcherData }); 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