Tobacco Etch Virus Protease Recombinant ( TEV )

Data sheet

Formulation

The rTEV contains 25mM Tris, 75mM NaCl, 5mM EDTA, 10mM GSH, 50% Glycerol.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

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

Protein 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

Expression host

Escherichia Coli.

Synonyms

rTEV, TEV, P1 protease.

Reagent Appearance

Sterile liquid formulation.

Stability

rTEV although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

Unit Definition

One unit is defined as the amount of enzyme needed to cleave 3 ug of fusion protein in 1 hour to 85 % completion at 30°C in a buffer containing 50 mM Tris-HCl, pH 8.0, 0.5 mM EDTA, and 1 mM DTT.