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Strep-tag
The ''Strep''-tag® system is a method which allows the purification and detection of proteins by affinity chromatography. The ''Strep''-tag is a synthetic peptide consisting of eight amino acids (Trp-Ser-His-Pro-Gln-Phe-Glu-Lys). This peptide sequence exhibits intrinsic affinity towards ''Strep''-Tactin, a specifically engineered streptavidin and can be N- or C- terminally fused to recombinant proteins. By exploiting the highly specific interaction, ''Strep''-tagged proteins can be isolated in one step from crude cell lysates. Because the ''Strep''-tag elutes under gentle, physiological conditions it is especially suited for generation of functional proteins.
== Development and biochemistry of the ''Strep''-tag ==
Streptavidin is a tetrameric protein expressed in ''Streptomyces avidinii''. Because of its high affinity for the vitamin h-biotin, Streptavidin is commonly used in the fields of molecular biology and biotechnology. The ''Strep''-tag was originally selected from a genetic library to specifically bind to a proteolytically truncated "core" version of streptavidin. Over the years, the ''Strep''-tag was systemically optimized, to permit a greater flexibility in the choice of attachment site. Further, its interaction partner, Streptavidin was also optimized to increase peptide-binding capacity, which resulted in the development of ''Strep''-Tactin. The binding affinity of Strep-tag to Strep-Tactin is nearly 100 times higher than to Streptavidin. The so called ''Strep''-tag system, consisting of ''Strep''-tag and ''Strep''-Tactin, has proven particularly useful for the functional isolation and analysis of protein complexes in proteome research.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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