TEV Protease

TEV Protease
The Tobacco etch virus (TEV) protease is one of the most popular proteases used to remove affinity tags from a recombinant protein. The TEV-protease recognition site is Glu-Asn-Leu- Tyr-Phe-Gln-Gly. Cleavage occurs between the Gln and Gly residues, resulting in a Gly at the amino terminus of the protein of interest. The TEV protease is active in 2.5% sucrose, 0.01% TRITON X-100, PMSF, aprotinin, and leu-peptin. However, 0.01 % SDS completely inhibits TEV.