Safety Information

HS Code 

3507909090

Recombinant Tobacco Etch Virus Protease Usage And Synthesis

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°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.

Source

Escherichia Coli

Background

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.

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