TEV Protease (active enzyme, HPLC verified)

TEV Protease is a recombinant form of Tobacco Etch Virus protease expressed in Escherichia coli. This protease is used to cleave affinity tags from fusion proteins. The TEV Protease recognition sequence with the highest catalytic efficiency is ENLYFQS/G, the cleavage site is between Q and S/G. TEV protease contains N-terminus His-tag, it can be removed by Ni2+ affinity resin for purification of the target protein.

Removal of affinity purification tags from fusion proteins.

1 unit of TEV Protease will cleave 2 µg of MBP-fusion protein to 95% completion in a total reaction volume of 10 µl in 1 hour at 30°C in 50 mM Tris-HCl (pH 7.5 @ 25°C) with 0.5 mM EDTA and 1 mM DTT.

>95% as determined by SDS-PAGE.

>95% as determined by SEC-HPLC.

>1 U/μL

Less than 1.0 EU per μg by the LAL method / rFC method.

Supplied as 0.2 μm filtered solution in 50 mM Tris, 250 mM NaCl, pH7.4 with glycerol as protectant.

Contact us for customized product form or formulation.

This product is supplied and shipped on dry ice.

• The product MUST be stored at -20°C or lower upon receipt;
• -20°C for 3 months under sterile conditions.

*The 10× Reaction Buffer provided in this kit contains DTT, a sulfhydryl reducing agent essential for maintaining enzyme activity. When employing the 10× Reaction Buffer exposed to prolonged storage or repeated freeze-thaw cycles, fresh 10 mM DTT should be supplemented to the Reaction Buffer to ensure maximal enzymatic activity, as oxidative degradation of DTT progressively compromises its reducing capacity.