Epitope Tags | Research Areas: Novus Biologicals

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5.1724696046-473375462.1712005244" style="margin: 0 10px;" target="_blank"><img alt="Novus Biologicals products are now on bio-techne.com" src="https://images.novusbio.com/design/ready-to-buy-novus-products-login.png" style="height:120px; width:940px" /></a></div> </div> </div> </div> <div class="clear"></div> <div class="ra-header"><img src="https://images.novusbio.com/design/ETHeader.png" class="ra-header" alt="Epitope Tags" /></div> </div> <div class="main grid_4"> <div class="ra-menu"><ul><li class="active"><a href="/research-areas/epitope-tags">Epitope Tags</a></li></ul></div><div class="ra-charities"><div class="ra-left-header">Charities</div><div class="ra-left-body"><span class="ra-button-span"><a href="mailto:marketing@novusbio.com?subject=Charity%20Submission%20for%20Epitope+Tags" class="ra-button">Submit a Charity</a></span><div class="clear"></div></div></div><div class="ra-events"><div class="ra-left-header">Events</div><div class="ra-left-body"><p class="ra-events-blurb"><span class="ra-events-image"> </span>Submit your event on Epitope Tags to be featured.</p><span class="ra-button-span"><a href="mailto:marketing@novusbio.com?subject=Event%20Submission%20for%20Epitope+Tags&body%3DEvent%20Name%3A%0ADescription%3A%0ADates%3A%0ATime%3A%0ALocation%3A%0AMore%20information%20URL%3A%0AImage%20%28please%20attach%20any%20relevant%20images%29" class="ra-button">Submit an Event</a></span><div class="clear"></div></div></div> </div> <div class="main grid_12"> <table width="700px"> <tr> <td valign="top"> <h1>What is an Epitope Tag?</h1> <p> Epitope tags such as V5, c-myc, and HA are biological structures, usually proteins, that are genetically engineered onto either the N or C terminus of a recombinant protein. Tags function as universal epitopes, easily detected by commercially available antibodies, and generally do not compromise the native structure or function of the protein. </p> <p> <img src="https://images.novusbio.com/design/epitopeTagsMain.png" alt="Epitope Tags"> </p> </td> </tr> <tr> <td> <table width="100%" cellpadding="6" cellspacing="6" border="0"> <tr> <td colspan="2"> <h2>What are epitope tags used for?</h2> <p> Tags and anti-tag antibodies are useful for many different immunoassays such as <a href="/application/western-blotting">western blotting</a>, <a href="/support/support-by-application/immunoprecipitation/protocol.html">immunoprecipitation</a>, <a href="/application/ihc">immunohistochemistry</a>, <a href="/application/icc">immunocytochemistry</a>, and flow cytometry. If your epitope tag ever loses antigenicity following deparaffinization and rehydration of formalin-fixed tissues in immunohistochemistry, try following our <a href="/epitope-retrieval">antigen retrieval protocol</a>. Epitope tags are the most economical way to detect newly discovered proteins for which specific antibodies are not yet available or for targets that are poorly immunogenic <sup>1</sup>. Additionally, epitope tags are also useful for affinity purification of target proteins from cell lysates <sup>2</sup>, enhancing the solubility of target proteins <sup>3</sup> protecting against intracellular protease cleavage (e.g. GST) <sup>4</sup>, and adding enzymatic function to a target protein <sup>5</sup>. </p> </td> </tr> <tr> <td valign="top" width="350px"> <p align="center"><strong>Western Blot</strong></p> <p align="center"> <img src="https://images.novusbio.com/design/WBV5ET.png" alt="V5 Epitope Tag Antibody"> </p> <p style="margin-left:40px; margin-right:40px;"> V5 Epitope Tag Antibody [<a href="/products/v5-epitope-tag-antibody_nb600-381">NB600-381</a>] - Detection of 200, 100, or 50 ng of E. coli whole cell lysate expressing a multi-tag fusion protein. </p> </td> <td valign="top" width="350px"> <p align="center"><strong>Flow Cytometry</strong></p> <p align="center"> <img src="https://images.novusbio.com/design/WBV5ETFlow.png" alt="V5 Epitope Tag Antibody"> </p> <p style="margin-left:40px; margin-right:40px;"> V5 Epitope Tag Antibody [<a href="/products/v5-epitope-tag-antibody-1036h_mab8926">MAB8926</a>] - HEK293 human embryonic kidney cell line transfected with V5-tagged proteins. </p> </td> </tr> <tr> <td valign="top"> <p align="center"><strong>Immunocytochemistry/Immunofluorescence</strong></p> <p align="center"> <img src="https://images.novusbio.com/design/HATagET.jpg" alt="HA Epitope Tag Antibody"> </p> <p style="margin-left:40px; margin-right:40px;"> HA Tag Antibody [<a href="/products/ha-tag-antibody_nb600-363">NB600-363</a>] - Detection of HA-tagged Tubulin in CHO cells transfected with mutant beta-tubulin cDNA encoding an HA epitope tag. </p> </td> <td valign="top"> <p align="center"><strong>Immunohistochemistry-Paraffin</strong></p> <p align="center"> <img src="https://images.novusbio.com/design/IHCParaET.jpg" alt="c-Myc Epitope Tag Antibody"> </p> <p style="margin-left:40px; margin-right:40px;"> c-Myc Antibody (9E10) [<a href="/products/c-myc-antibody-9e10_nb600-302">NB600-302</a>] - c-Myc was detected in immersion fixed paraffin-embedded sections of human breast cancer using anti-human mouse monoclonal antibody聽 </p> </td> </tr> <tr> <td valign="top" colspan="2"> <p align="center"><strong>Affinity Purification</strong></p> <p align="center"> <img src="https://images.novusbio.com/design/ETAffinity.jpg" alt="Ni-NTA Affinity Purification Column"> </p> <p style="margin-left:120px; margin-right:120px;"> HA, His, DYKDDDDK, and V5 are commonly used epitope tags for affinity purification. </p> </td> </tr> </table> </td> </tr> <tr> <td> <h2>Choosing Your Epitope Tag</h2> <p> No single epitope tag is useful for every application --- when choosing a tag, consider how the size and charge of the tag will ultimately affect the protein鈥檚 function, solubility and downstream analysis. Multiple tags can be added to a single protein to get enhanced functionality, however, this increases the risk of losing native function, compromising the original structure, or altering protein trafficking <sup>6,7,8</sup>. </p> </td> </tr> <tr> <td valign="top"> <table cellpadding="4" cellspacing="4" border="0" width="700px"> <tr bgcolor="#005F9E"> <td valign="top"> <span style="color: #FFFFFF; font-weight: bold;">Epitope Tags</span> </td> <td valign="top"> <span style="color: #FFFFFF; font-weight: bold;">Length (Sequence)<br/>(kDa)</span> </td> <td valign="top"> <span style="color: #FFFFFF; font-weight: bold;">Alternate Names</span> </td> <td valign="top"> <span style="color: #FFFFFF; font-weight: bold;">Source</span> </td> <td valign="top"> <span style="color: #FFFFFF; font-weight: bold;">Notes</span> </td> <td>   </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/ha-tag">HA</a> </td> <td valign="top"> YPYDVPDYA </td> <td valign="top"> Hemagglutinin </td> <td valign="top"> Amino acids 98-106 of Human influenza hemagglutin which is a surface glycoprotein required for the infectivity of the human virus </td> <td valign="top"> Strong immunoreactive epitope and mild elution conditions makes it a popular epitope tag to purify tagged proteins <sup>10</sup>; useful in mammalian expression systems <sup>9</sup>; not suitable for detection or purification of proteins from apoptotic cells since it is cleaved by Caspase-3 and / or Caspase-7 after its sequence DVPD, causing it to lose its immunoreactivity <sup>11</sup> </td> <td>   </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/his-tag">HIS</a> </td> <td valign="top"> H-H-H-H-H-H </td> <td valign="top"> 6 His<br/> 6X-His<br/> HHHHHH tag<br/> polyHistidine<br/> hexa-histidine tag </td> <td valign="top"> Synthetic </td> <td valign="top"> Most common purification tag; Purification via Nickel, Cobalt, Copper, or Zinc column (Find Nickel and Cobalt Resin <a href="/search?keywords=amintra">here</a>); Regenerable affinity matrix <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/dykddddk-epitope-tag">FLAG</a> <sup>TM</sup> </td> <td valign="top"> DYKDDDDK </td> <td valign="top"> Ty 1 Tag<br/> DDK tag<br/> DDDDK tag<br/> DYKDDDDK tag<br/> xxxDDDDK epitope tag<br/> Enterokinase Cleavage Site tag<br/> ECS tag<br/> Ty 1 </td> <td valign="top"> Synthetic </td> <td valign="top"> Hydrophilic epitope tag introduced to purify fusion proteins <sup>10</sup>; Contains internal Enterokinase cleavage site </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/au1-epitope-tag">AU1</a> </td> <td valign="top"> DTYRYI </td> <td valign="top">   </td> <td valign="top"> Major capsid protein of bovine papillomavirus-1 (BPV-1) </td> <td valign="top"> Not recommended for affinity purification as protein properties may get altered during low pH elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/au5-epitope-tag">AU5</a> </td> <td valign="top"> TDFYLK </td> <td valign="top">   </td> <td valign="top"> Major capsid protein of bovine paillomavirus-1 (BPV-1) </td> <td valign="top"> Not recommended for affinity purification as protein properties may get altered during low pH elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/myc-epitope-tag">Myc</a> </td> <td valign="top"> EQKLISEEDL </td> <td valign="top">   </td> <td valign="top"> Amino acid residues 410-419 of Human c-Myc </td> <td valign="top"> Not recommended for affinity purification as protein properties may get altered during low pH elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/glu-glu-epitope-tag">Glu-Glu</a> </td> <td valign="top"> EYMPME </td> <td valign="top">   </td> <td valign="top"> Amino acid residues 314-319 of middle T antigen of mouse polyomavirus </td> <td valign="top"> Not recommended for affinity purification as protein properties may get altered during low pH or 30掳C elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/ollas-epitope-tag">OLLAS</a> </td> <td valign="top"> SGFANELGPRLMGK </td> <td valign="top"> OLLA-2<br/> E.coli OmpF Linker and mouse<br/> Langerin fusion Sequence </td> <td valign="top"> 14 amino acid sequence residing in the junction between E. coli OmpF protein (OFL/OmpF linker) and mLangerin extracellular domain. </td> <td valign="top"> The OLLAS epitope tag is detectable at approximately 100-fold lower levels than similar commercially available tags </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/t7-epitope-tag">T7</a> </td> <td valign="top"> MASMTGGQQMG </td> <td valign="top">   </td> <td valign="top"> 11 amino acid N-terminus of Bacteriophage T7 gene 10 </td> <td valign="top"> May help increase expression; Not recommended for affinity purification as protein properties may get altered during low pH elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/v5-epitope-tag">V5</a> </td> <td valign="top"> GKPIPNPLLGLDST </td> <td valign="top"> Parainfluenza virus 5 V/P tag<br/> Paramyxovirus SV5 tag </td> <td valign="top"> Amino acid residues 95 to 108 of RNA polymerase alpha subunit of simion virus 5 </td> <td valign="top"> Some cross reactivity may occur when using mammalian expression systems; Recommended for affinity purification in combination with His-tag <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/vsv-g-epitope-tag">VSV-G</a> </td> <td valign="top"> YTDIEMNRLGK </td> <td valign="top"> Vesicular stomatitis virus glycoprotein tag </td> <td valign="top"> 11 amino acid C-terminus of the Vesicular Stomatitis viral glycoprotein </td> <td valign="top"> Not recommended for affinity purification as protein properties may get altered during low pH elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/e-tag-epitope-tag">E-Tag</a> </td> <td valign="top"> GAPVPYPDPLEPR </td> <td valign="top">   </td> <td valign="top"> Bone hormone osteocalcin produced by osteoblasts </td> <td valign="top"> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/s-tag-epitope-tag">S-Tag</a> </td> <td valign="top"> KETAAAKFERQHMDS </td> <td valign="top"> S 7 Epitope tag </td> <td valign="top"> 15 amino acid sequence at N-terminus of RNase A </td> <td valign="top"> Not recommended for affinity purification as protein properties may get altered during low pH elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/avi-epitope-tag">Avi</a> </td> <td valign="top"> CGLNDIFEAQKIEWHE </td> <td valign="top">   </td> <td valign="top"> Synthetic </td> <td valign="top"> Allows for either the in-vivo or in-vitro enzymatic biotinylation by the biotin ligase BirA from E. coli; May lead to decreased solubility <sup>12</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/hsv-tag">HSV</a> </td> <td valign="top"> SQPELAPEDPED </td> <td valign="top">   </td> <td valign="top"> Herpes Simplex Virus tag </td> <td valign="top"> C-terminal placement only; Not recommended for affinity purification as protein properties may get altered during low pH elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/kt3-epitope-tag">KT3</a> </td> <td valign="top"> KPPTPPPEPET </td> <td valign="top">   </td> <td valign="top"> Simian Virus 40 (SV40) large T-antigen </td> <td valign="top"> Not recommended for affinity purification as protein properties may get altered during low pH elution step <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/tk15-epitope-tag">TK15</a> </td> <td valign="top"> (R/K)TV(I/L)HGESNSA(I/L)(I/L)(I/L)GPR </td> <td valign="top">   </td> <td valign="top"> Xenopus Orc1p </td> <td valign="top"> No cross-reactivity with mammalian or bacterial proteins has been detected; Used for immunoaffinity purification <sup>16</sup> </td> <td valign="top">   </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #f3f3f3;"> <td valign="top"> <a href="/common-name/strep-ii-tag">Strep-tag II</a> </td> <td valign="top"> WSHPQFEK or AWAHPQPGG </td> <td valign="top">   </td> <td valign="top"> Synthetic </td> <td valign="top"> Regenerable affinity matrix; compatible with purifications requiring anaerobic conditions <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #C5CFDF;"> <td valign="top"> <a href="/common-name/beta-galactosidase">Beta-Galactosidase</a> </td> <td valign="top"> 116 kDa </td> <td valign="top">   </td> <td valign="top"> Enzyme coded by lac z gene in the lac operon of E. coli </td> <td valign="top"> Metalloenzyme that splits lactose into glucose and galactose; Allows for enzymatic protein quantification assays; May protect from proteolytic activity; May decrease solubility; Tag may form tetramers in solution <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #C5CFDF;"> <td valign="top"> <a href="/common-name/maltose-binding-protein">Maltose Binding Protein</a> </td> <td valign="top"> 42.5 kDa </td> <td valign="top"> MBP </td> <td valign="top"> Maltose/maltodextrin system of E. coli </td> <td valign="top"> Amylose purification column compatible with non-ionizing detergents and high salt but not reducing agents; Large size; N-terminal tagging may reduce translation efficiency; <sup>9</sup>; Enhanced protein production <sup>13</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #C5CFDF;"> <td valign="top"> <a href="/products/calmodulin-antibody-c16t_nbp2-29791">Calmodulin Binding Protein (CBP)</a> </td> <td valign="top"> 4 kDa </td> <td valign="top">   </td> <td valign="top"> Cytoplasm of all Eukaryotic cells </td> <td valign="top"> No cross-reaction with any endogenous E.coli proteins; High yield affinity Calmodulin column purification; Not useful for purification from eukaryotic cells; N-terminus tagging may reduce translation efficiency <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #C5CFDF;"> <td valign="top"> <a href="/common-name/gfp">Green Fluorescent Protein (GFP)</a> </td> <td valign="top"> 27 kDa </td> <td valign="top">   </td> <td valign="top"> Jellyfish Aequorea Victoria </td> <td valign="top"> Major excitation peak at a wavelength of 395 nm and a minor one at 475 nm; emission peak is at 509 nm; Detectable in living organisms without antibody; Can sometimes be non-specifically directed to nucleus; Useful to monitor protein-protein interactions by FRET; Very large; Dimerization may occur <sup>9</sup>; Useful in protein-folding assays <sup>5</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #C5CFDF;"> <td valign="top"> <a href="/common-name/gst-epitope-tag">Glutathione S Transferase (GST)</a> </td> <td valign="top"> 27 kDa </td> <td valign="top">   </td> <td valign="top"> Eukaryotes and Prokaryotes </td> <td valign="top"> Affinity purification via relatively reusable glutathione conjugated columns; purification under native conditions only; Highly antigenic; may cause insolubility; may dimerize <sup>9</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #C5CFDF;"> <td valign="top"> <a href="/common-name/mcherry">mCherry</a> </td> <td valign="top"> 28 kDa </td> <td valign="top"> DsRED<br/> Red Fluorescent Protein<br/> RFP </td> <td valign="top"> Disc corals of Discosoma species </td> <td valign="top"> Useful to monitor protein-protein interactions by FRET; Excitation maximum at 587 nm and an emission maximum at 610 nm </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #C5CFDF;"> <td valign="top"> <a href="/common-name/igg-fc">Fc-Fusion Proteins</a> </td> <td valign="top">   </td> <td valign="top"> Fc chimeric fusion proteins<br/> Fc-Ig's<br/> Fc-tag protein<br/> Ig-based Chimeric fusion protein </td> <td valign="top"> Fc domain of IgG Antibody </td> <td valign="top"> The Fc domain can improve the solubility and stability of the tagged protein both in vitro and in vivo; Easy cost-effective purification by protein-G/A affinity chromatography <sup>14</sup> </td> <td valign="top"> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px; background-color: #C5CFDF;"> <td valign="top"> <a href="/common-name/thioredoxin-1">Thioredoxin</a> </td> <td valign="top"> 12 kDa </td> <td valign="top"> Trx<br/> TRDX </td> <td valign="top"> Found in all organisms; Encoded by TXN and TXN2 genes in humans </td> <td valign="top"> Can enhance the solubility of tagged protein <sup>15</sup> </td> <td valign="top"> </td> </tr> <tr> <td colspan="3" style="background-color: #f3f3f3;"> Peptide tags in grey. </td> <td colspan="3" style="background-color: #C5CFDF;"> Fusion Proteins in blue. </td> </tr> </table> <br/><br/> <p align="center"> <a href="/search?keywords=epitope+tags" class="link_button">View All Epitope Tags</a> </p> <br/> <h2>Cleavage Sites</h2> <p> Tags are removable by proteolytic enzymes that cleave the tag from the protein of interest, and generally the cleavage site needs to be engineered between the tag and the protein. Consider utilizing these commonly used proteases in your experiments: (Note: // denotes cleavage site) </p> <br/><br/> <table cellpadding="4" cellspacing="4" border="0" width="100%"> <tr bgcolor="#005f9e"> <td valign="top"> <span style="color: #FFFFFF; font-weight: bold;">Protease</span> </td> <td valign="top"> <span style="color: #FFFFFF; font-weight: bold;">Recognition Site</span> </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px;"> <td valign="top"> <a href="/proteins/tev-protease">TEV Protease</a> </td> <td valign="top"> Glu-Asn-Leu-Tyr-Phe-Gln-Gly//Ser </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px;"> <td valign="top"> <a href="/search?keywords=thrombin&category=Peptides%20and%20Proteins&applications=Enzyme%20Activity&common_name=Coagulation%20Factor%20II/Thrombin">Thrombin</a> </td> <td valign="top"> Leu-Val-Pro-Arg//Gly-Ser </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px;"> <td valign="top"> <a href="/proteins/coagulation-factor-x">Factor Xa</a> </td> <td valign="top"> Ile-(Glu/Asp)-Gly-Arg// <br/> Occasionally Gly-Arg// </td> </tr> <tr style="border-bottom-style: solid; border-color:#005f9e; border-width: 1px;"> <td valign="top"> <a href="/search?keywords=Enteropeptidase&category=Peptides%20and%20Proteins&applications=Enzyme%20Activity">Enteropeptidase/Enterokinase</a> </td> <td valign="top"> Asp-Asp-Asp-Asp-Lys// </td> </tr> </table> <br/><br/> <p> <strong>References</strong><br/> 1. BioTechniques, Vol. 44, No. 5, Mini-Review: Epitope Tagging; Bill Brizzard; Published online: 16 May 2018, https://doi.org/10.2144/000112841 <br/> 2, Kimple ME, Brill AL, Pasker RL. Overview of affinity tags for protein purification.聽Curr Protoc Protein Sci. 2013;73:Unit 9.9. Published 2013 Sep 24. doi:10.1002/0471140864.ps0909s73 <br/> 3. Walls D., Loughran S.T. (2011) Tagging Recombinant Proteins to Enhance Solubility and Aid Purification. In: Walls D., Loughran S. (eds) Protein Chromatography. Methods in Molecular Biology (Methods and Protocols), vol 681. Humana Press <br/> 4. Terpe, K. Appl Microbiol Biotechnol (2003) 60: 523. https://doi.org/10.1007/s00253-002-1158-6 <br/> 5. Nat Biotechnol.聽1999 Jul;17(7):691-5.Rapid protein-folding assay using green fluorescent protein. Waldo GS1,聽Standish BM,聽Berendzen J,聽Terwilliger TC. <br/> 6. Sabourin, M. , Tuzon, C. T., Fisher, T. S. and Zakian, V. A. (2007), A flexible protein linker improves the function of epitope鈥恡agged proteins in聽Saccharomyces cerevisiae. Yeast, 24: 39-45. doi:10.1002/yea.1431 <br/> 7. Zordan RE, Beliveau BJ, Trow JA, Craig NL, Cormack BP. Avoiding the ends: internal epitope tagging of proteins using transposon Tn7.聽Genetics. 2015;200(1):47-58. <br/> 8. Maue, R. A. (2007), Understanding ion channel biology using epitope tags: Progress, pitfalls, and promise. J. Cell. Physiol., 213: 618-625. doi:10.1002/jcp.21259 <br/> 9. Kimple ME, Brill AL, Pasker RL. Overview of affinity tags for protein purification.聽Curr Protoc Protein Sci. 2013;73:Unit 9.9. Published 2013 Sep 24. doi:10.1002/0471140864.ps0909s73 <br/> 10. Zhao X, Li G, Liang S. Several affinity tags commonly used in chromatographic purification.聽J Anal Methods Chem. 2013;2013:581093. <br/> 11. Nat Methods.聽2007 Feb;4(2):107-8. The HA tag is cleaved and loses immunoreactivity during apoptosis. Schembri L,聽Dalibart R,聽Tomasello F,聽Legembre P,聽Ichas F,聽De Giorgi F <br/> 12. Mukherjee S, Ura M, Hoey RJ, Kossiakoff AA. A New Versatile Immobilization Tag Based on the Ultra High Affinity and Reversibility of the Calmodulin-Calmodulin Binding Peptide Interaction.聽J Mol Biol. 2015;427(16):2707-25. <br/> 13. Reuten R, Nikodemus D, Oliveira MB, et al. Maltose-Binding Protein (MBP), a Secretion-Enhancing Tag for Mammalian Protein Expression Systems.聽PLoS One. 2016;11(3):e0152386. Published 2016 Mar 30. doi:10.1371/journal.pone.0152386 <br/> 14. Exp Cell Res.聽2011 May 15;317(9):1261-9. doi: 10.1016/j.yexcr.2011.02.013. Epub 2011 Mar 1. Introduction to current and future protein therapeutics: a protein engineering perspective. Carter PJ. <br/> 15. J Biol Chem.聽1995 Oct 27;270(43):25328-31. Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. Yasukawa T1,聽Kanei-Ishii C,聽Maekawa T,聽Fujimoto J,聽Yamamoto T,聽Ishii S. <br/> 16. J Biol Chem. 1998 Dec 4;273(49):32421-9. The Orc4p and Orc5p subunits of the Xenopus and human origin recognition complex are related to Orc1p and Cdc6p. Tugal T1, Zou-Yang XH, Gavin K, Pappin D, Canas B, Kobayashi R, Hunt T, Stillman B. </p> <br/> <br/> <p align="center"> *FLAG is a trademark of Sigma Aldrich </p> </td> </tr> </table> <br/><br/> <div class="ra-product-block"></div> </div> </div> <div id="novus_footer_line"></div>  </div> <div class="container_16"> <div id="footer"> <div class="grid_16 text_center"> <div class="fp_horzline"></div> </div> <div class="clear"></div> <div class="grid_16"> <table class="footer_boxes"> <tr> <th>Popular Products</th> <th>Company Information</th> <th>Support</th> <th>Stay Connected</th> </tr> <tr> <td> <ul class='links'><li><a href="/productsearch/novus">Antibodies</a></li><li><a href="/product-type/secondary-antibodies">Secondary Antibodies</a></li><li><a href="/product-type/isotype-controls">Isotype Controls</a></li><li><a href="/product-type/peptides-and-proteins">Proteins and Peptides</a></li><li><a href="/product-type/elisa-kits">ELISA Kits</a></li><li><a href="/samplesize">Sample Size</a></li><li><a href="https://www.novusbio.com/new-product-information-page.html">New Products</a></li> </ul> </td> <td> <ul class='links'><li><a href="/about.html">About Us</a></li><li><a href="https://www.bio-techne.com/about/careers">Careers</a></li><li><a href="/guarantee">Novus Guarantee</a></li><li><a href="/about/contact-us.html">Contact Us</a></li><li><a href="/about/novus-team.html">Our Team</a></li> </ul> </td> <td> <ul class='links'><li><a href="/support/technical-support.html">Technical Support</a></li><li><a href="/support/faqs.html">FAQs</a></li><li><a href="/webform/help-finding-antibodies">Help Finding Antibodies</a></li><li><a href="/support/support-by-application.html">Protocols</a></li> </ul> </td> <td id="footer_social_links"> </td> </tr> </table> </div> <div class="clear"></div> <div class="grid_16"> <div id="GTS_CONTAINER" style="float: right;margin-top: 10px;"></div> <div id="footer_officeinfo"> </div> <div class="fp_horzline"></div> <div class="footer_othersites"> <p>Visit our other sites</p> <a href="https://www.bio-techne.com/" target="_blank"><div class="fp_biotechne"></div></a> <a href="https://www.rndsystems.com/"><div class="fp_rnd"></div></a> <a href="https://www.novusbio.com/" target="_blank"><div class="fp_novus"></div></a> <a href="https://www.tocris.com/" target="_blank"><div class="fp_tocris"></div></a> <a href="https://www.bio-techne.com/brands/proteinsimple" target="_blank"><div class="fp_proteinSimple"></div></a> <a href="http://www.biospacific.com/" target="_blank"><div class="fp_biospacific"></div></a>  <a href="http://www.acdbio.com/" target="_blank"><div class="fp_acd"></div></a> <a href="https://www.rndheme.com/" target="_blank"><div class="fp_rndcc"></div></a> </div> <div class="text_center"> <div class="fp_horzline"></div> </div> <div class="copyright">©2024 Novus Biologicals, All Rights Reserved.</div> <div class="footer_legal"> <ul class="links"><li class="menu-47946 first"><a href="/support/customer-service/privacy-policy.html" title="">Privacy Policy</a></li> <li class="menu-47956"><a href="/novus-bio-sitemap.html" title="">Sitemap</a></li> <li class="menu-47951"><a href="/about/contact-us.html" title="">Contact Us</a></li> <li class="menu-47941 last"><a href="/support/customer-service/terms.html" title="">Terms & Conditions</a></li> </ul> </div> <div class="clear"></div> </div> </div> </div> <script type="text/javascript"> <![CDATA[//><!]]> </script> <script type="text/javascript">window.NREUM||(NREUM={});NREUM.info={"beacon":"bam.nr-data.net","licenseKey":"76fb58fb05","applicationID":"788348554,30870807","transactionName":"YFdbZBFZXxdWAhAMVlkdeFMXUV4KGA8LAVxoQlhXBmdHDVIW","queueTime":15,"applicationTime":196,"atts":"TBBYEllDTBk=","errorBeacon":"bam.nr-data.net","agent":""}</script></body> </html>

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