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Nature Methods - 3, 1013 - 1019 (2006)
Published online: 22 October 2006; Corrected online: 6 October 2006 | doi:10.1038/nmeth968

An efficient tandem affinity purification procedure for interaction proteomics in mammalian cells

Tilmann Bürckstümmer, Keiryn L Bennett, Adrijana Preradovic, Gregor Schütze, Oliver Hantschel, Giulio Superti-Furga & Angela Bauch

 
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Figure 1. Schematic representation of TAP.
(a) Schematics of the four TAP tags that were obtained by permutation of protein A and protein G with CBP and SBP. (b) Overview of the TAP protocol. During the first step, TAP-tagged proteins are sequestered by IgG sepharose (1) and released by TEV-protease cleavage (2). TEV protease–cleaved proteins are then bound to streptavidin sepharose (3) and eluted with 1 mM biotin (4). (c) Nucleotide and amino-acid sequence of the GS-TAP tag which is comprised of protein G and SBP.

 
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