期刊
JOURNAL OF ANALYTICAL METHODS IN CHEMISTRY
卷 2013, 期 -, 页码 -出版社
HINDAWI LTD
DOI: 10.1155/2013/581093
关键词
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资金
- National Key Basic Research Program of China [2011CB910703, 2013CB911303]
- National 863 High Tech Foundation [SS2014AA020608]
- Natural Science Foundation of China [30800581, 31071235]
- New Century Excellent Talents in University [NCET-10-0595]
- Specialized Research Fund for the Doctoral Program of Higher Education [20120181110025]
Affinity tags have become powerful tools from basic biological research to structural and functional proteomics. They were widely used to facilitate the purification and detection of proteins of interest, as well as the separation of protein complexes. Here, we mainly discuss the benefits and drawbacks of several affinity or epitope tags frequently used, including hexahistidine tag, FLAG tag, Strep II tag, streptavidin-binding peptide (SBP) tag, calmodulin-binding peptide (CBP), glutathione S-transferase (GST), maltose-binding protein (MBP), S-tag, HA tag, and c-Myc tag. In some cases, a large-size affinity tag, such as GST or MBP, can significantly impact on the structure and biological activity of the fusion partner protein. So it is usually necessary to excise the tag by protease. The most commonly used endopeptidases are enterokinase, factor Xa, thrombin, tobacco etch virus, and human rhinovirus 3C protease. The proteolysis features of these proteases are described in order to provide a general guidance on the proteolytic removal of the affinity tags.
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