Strep-tag

The Strep-tag system is a method which allows the purification and detection of proteins by affinity chromatography. The Strep-tag II 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 the generation of functional proteins.[1][2]

Strep-tag, Twin-Strep-tag and Strep-Tactin are registered trademarks of IBA Lifesciences GmbH.

  1. ^ Schmidt, Thomas GM; Skerra, Arne (2007). "The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins". Nature Protocols. 2 (6): 1528–35. doi:10.1038/nprot.2007.209. PMID 17571060. S2CID 25209313.
  2. ^ Skerra, A; Schmidt, TG (2000). "Use of the Strep- tag and streptavidin for detection and purification of recombinant proteins". Applications of Chimeric Genes and Hybrid Proteins Part A: Gene Expression and Protein Purification. Methods in Enzymology. Vol. 326. pp. 271–304. doi:10.1016/S0076-6879(00)26060-6. ISBN 978-0-12-182227-9. PMID 11036648.