CRP08121

Recombinant Tobacco Etch Virus Protease produced in E.coli I has a molecular mass of approximately 27 kDa.

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. rTEV contains both GST and His tag, and can be easily removed from the digestion reaction by affinity chromatography.

 Synonyms

rTEV, TEV, P1 protease

>95% by SDS-PAGE and HPLC analyses.

One unit of rTEV cleaves ≥85% of 3 μg control substrate in 1 h at 30°C.

0.50 M Tris-HCl (pH 8.0), 10 mM DTT, 5 mM EDTA.

A number of variables can be changed to optimize the cleavage of any specific protein. The amount of rTEV, the temperature of the incubation, and the time needed for cleavage may be examined. If the protein of interest is heat-labile, then 4°C incubations are recommended. Reactions at 4°C will require longer incubation time and/or more rTEV.

The rTEV (1000 IU/ml) contains 0.50 M Tris-HCl pH 8.0, 10mM DTT and 5 mM EDTA.

rTEV although stable at 10°C for 5 days, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.

Store rTEV at -70°C for long term or at -20°C for < 6 months.