Recombinant Tobacco Etch Virus Protease

Source : Escherichia Coli. Recombinant TEV Protease (rTEV) is a site-specific protease purified from E. coli. The protease can be used for the removal of affinity tags from fusion proteins. The seven-amino-acid recognition site for rTEV is Glu-Asn-Leu-Tyr-Phe-Gln-Gly with cleavage occurring between Gln and Gly. The optimal temperature for cleavage is 30°C; however, the enzyme can be used at temperatures as low as 4°C. The rTEV contains His tag.The rTEV is purified by proprietary chromatographic techniques. TEV protease is the common name for the 27 kDa catalytic domain of the Nuclear Inclusion a (NIa) protein encoded by the tobacco etch virus (TEV) . Because its sequence specificity is far more stringent than that of factor Xa, thrombin, or enterokinase, TEV protease is a very useful reagent for cleaving fusion proteins. TEV protease recognizes a linear epitope of the general form E-Xaa-Xaa-Y -Xaa-Q- (G/S), with cleavage occurring between Q and G or Q and S. The most commonly used sequence is ENLYFQG.