链霉亲和素
生物素
亲和层析
生物素化
生物化学
肽
化学
细胞
细胞培养
生物分子
组合化学
分子生物学
生物
遗传学
酶
作者
Torben Schmidt,Arne Skerra
出处
期刊:Methods in molecular biology
日期:2015-01-01
卷期号:: 83-95
被引量:14
标识
DOI:10.1007/978-1-4939-2447-9_8
摘要
The Strep-tag—or its improved version Strep-tagII—is an eight amino acid sequence that can be easily fused or conjugated to any protein or peptide of interest and that was engineered for high affinity toward streptavidin, which otherwise is widely known as a tight biotin-binding reagent. Especially in combination with immobilized Strep-Tactin, a mutant streptavidin specifically optimized toward the Strep-tagII, this system enables the facile one-step affinity purification of various biomolecules, including oligomeric and even membrane proteins. The Strep-tagII/Strep-Tactin interaction shows exquisite specificity, thus allowing efficient separation from host cell proteins, and it can be reversed simply by addition of biotin (or a suitable derivative thereof, such as desthiobiotin). Therefore, this system has become very popular for the highly efficient affinity chromatography under biochemically mild conditions. Here, we describe the purification of Strep-tagged proteins from mammalian cell lysates and cell culture supernatants.
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