TEV protease (TEVp)
Recombinant version of the catalytic domain of the nuclear inclusion protein of Tobacco Etch Virus.
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TEV protease cleaves proteins at a specific site of seven amino acid residues of the following composition: Glu-Asn-Leu-Tyr-Phe-Glu- X (ENLYFQ-X). In this case, the seventh amino acid residue can be one of six: serine (S), glycine (G), alanine (A), methionine (M), cysteine ??(C) or histidine (H) [1]. Cleavage occurs between the glutamine and X amino acid residues (Gln-X).
TEV protease can be used to cleave fused recombinant polypeptides that have a protease recognition site between the leader fragment and the target protein. The presence of a histidine tag in TEV protease allows purification of the target protein from the enzyme using metal chelate affinity chromatography.
