UNIT 19.20 Strep/FLAG Tandem Affinity Purification (SF-TAP) to Study Protein Interactions
Published Online: 1 AUG 2009
Copyright © 2009 by John Wiley & Sons, Inc.
Lab Protocol Title
Current Protocols in Protein Science
How to Cite
Gloeckner, C. J., Boldt, K. and Ueffing, M. 2009. Strep/FLAG Tandem Affinity Purification (SF-TAP) to Study Protein Interactions. Current Protocols in Protein Science. 57:19.20:19.20.1–19.20.19.
- Published Online: 1 AUG 2009
- Published Print: AUG 2009
In recent years, several methods have been developed to analyze protein-protein interactions under native conditions. One of them, tandem affinity purification (TAP), combines two affinity-purification steps to allow isolation of high-purity protein complexes. This unit presents a methodological workflow based on an SF-TAP tag comprising a doublet Strep-tag II and a FLAG moiety optimized for rapid as well as efficient tandem affinity purification of native proteins and protein complexes in higher eukaryotic cells. Depending on the stringency of purification conditions, SF-TAP allows both the isolation of a single tagged-fusion protein of interest and purification of protein complexes under native conditions. Curr. Protoc. Protein Sci. 57:19.20.1-19.20.19. © 2009 by John Wiley & Sons, Inc.
- tandem affinity purification;
- protein complexes