TAP-Tag Monoclonal Antibody

Tandem affinity purification (TAP) is a purification technique for studying proteinprotein interactions. It involves creating a fusion protein with a designed piece, the TAP tag, on the end. The original TAP method involves the fusion of the TAP tag to the C-terminus of the protein under study. The TAP tag consists of calmodulin binding peptide (CBP) from the N-terminal, followed by tobacco etch virus protease (TEV protease) cleavage site and Protein A, which binds tightly to IgG. The relative order of the modules of the tag is important because Protein A needs to be at the extreme end of the fusion protein so that the entire complex can be retrieved using an IgG matrix.