TEV Protease (with His-tag)

TEV Protease (with His-tag) is derived from the tobacco etch virus and has been genetically engineered for recombinant expression in Escherichia coli. It retains the natural enzymatic activity of TEV protease while exhibiting improved tolerance to variations in pH and temperature. TEV Protease is a highly specific cysteine protease, widely utilized for the removal of affinity tags from fusion proteins. It precisely recognizes the seven-amino-acid sequence EXXYXQ↓ (G/S) and cleaves between the glutamine and glycine/serine residues. The most commonly recognized sequence is Glu-Asn-Leu-Tyr-Phe-Gln↓Gly. The inclusion of a His-tag at the N-terminus of TEV Protease allows for its efficient removal via Ni-affinity chromatography following digestion, thereby simplifying the purification of the target protein.