The recombinant Endotoxin-Free TEV Protease is made from E. coli. It is a 28.5 kDa protein containing an enhanced form of a catalytic domain of the N1a protein of Tobacco etch virus (TEV), and is N-terminal His tagged and C-terminal polyArg tagged. The TEV protease recognizes the cleavage site of Glu-Asn-Leu-Tyr-Phe-Gln-Gly and cleaves between Gln and Gly. The TEV protease has a robust activity at 4ºC with high specificity and excellent stability.
TEV Protease cleaves >90% of the substrate at a protease to target protein ratio of 1:30-1:100 (w/w) O/N at 4ºC. The cleavage is performed during dialysis in a buffer of 25 mM Tris-HCl, pH7.5, 150-500 mM NaCl, 1 mM DTT and 5 mM β-Mercaptoethanol.
0.2 µm filtered solution of 25 mM Tris-HCl, pH7.5, 0.05 M NaCl, 1 mM DTT, 0.5 mM EDTA, 10% glycerol
This protein should be stored below < -20ºC