Tobacco Etch Virus Protease (TEV) Recombinant Protein

Description: 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 degree C; however, the enzyme can be used at temperatures as low as 4 degree C. The rTEV contains His tag.The rTEV is purified by proprietary chromatographic techniques.

Introduction: 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.

Small volumes of TEV recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS143255 is a recombinant protein targeting TEV. Also known as Recombinant Tobacco Etch Virus Protease. Host: E Coli.