TEV protease, encoded by the Tobacco Etch Virus (TEV), is a 27 kDa catalytic domain of the Nuclear Inclusion a (NIa) protein encoded by the virus (TEV). It is widely used for cleaving fusion proteins because of its sequence specificity. It recognizes a linear epitope of the general form E-Xaa-Xaa-Y-Xaa-Q-(G/S). Cleavage occurs between Q and G or Q and S. The structure of TEV protease is similar to that of of the serine protease family. Like serine proteases, TEV protease utilizes a catalytic triad of residues to hydrolyze peptide bonds. The distinguishing feature of TEV protease, however, is that instead of the serine nucleophile in the triad Ser-Asp-His, there is a cysteine, which may explain the resistance of TEV protease to protease inhibitors which are commonly used. The strain used is the autoinactivation-resistant mutant S219V. The catalytic activity of the S219V mutant is approximately 2 fold greater than that of the wild-type protease.
This protein-A purified antibody was prepared from whole rabbit serum produced by repeated immunizations with recombinant MBP-and-poly-His-tagged autoinactivation-resistant mutant TEV Protease.