Recombinant Tobacco Etch Virus rTEV Protease

Virus

E.coli

28 kDa (Reducing)

Liquid

20mM Tris-HCl, pH8.0, 150mM NaCl, 1mM EDTA, 5mM DTT, 50%(v/v) Glycerol

1U/μL, 10U/μL

＞98% SDS-PAGE & RP-HPLC

＜1EU/μg(LAL)

unconjugated

One unit of TEV protease cleaves ≥85% of 3 μg of control substrate in 1 hour at pH 8.0 at 30°C.

Within 1 month, 2 to 8 °C under sterile conditions after reconstitution. 12 months from date of receipt, -20 to -80 °C as supplied. Avoid repeated freeze-thaw cycles.

The tobacco etch virus (TEV) protease is a useful tool for the removal of fusion tags from recombinant proteins. TEV protease has a strict 7 amino acid cleavage recognition sequence of Glu-Asn-Leu-Tyr-Phe-Gln-Gly/Ser [ENLYFQ(G/S)] and cleavage occurs between the Gln and Gly/Ser residues, The most commonly used sequence is ENLYFQG. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin. Recombinant Tobacco Etch Virus Protease (rTEV) has (NIa) protease catalytic domain which corresponds to a molecular weight of 28 kDa. It is unique with high specificity and is active at low temperature. rTEV Protease has a 6*His-tag for easy removal from a reaction using nickel affinity resins and has been engineered to improve thermal stability and decrease autolysis.