TEV Protease

Product Description: TEV Protease is a recombinant protease derived from Tobacco Etch Virus (TEV). The engineered variant demonstrates improved stability compared with native TEV protease and is commonly used to remove affinity tags from purified fusion proteins. TEV protease possesses high site specificity and recognizes the seven-amino-acid sequence EXXYXQ(G/S), with the most widely used motif being ENLYFQG. Cleavage occurs between glutamine and glycine or serine. The protease can cleave multiple amino acid sequences at the G/S (P1') site, generating a desired N-terminal amino acid on the cleaved fusion fragment. This protease exhibits optimal activity at pH 7.0 and 30℃, yet remains active over a broad range of pH 6.0–8.5 and 4–30℃, enabling flexible reaction conditions customized for target proteins.

Recombinant TEV protease carries an N-terminal His-tag, allowing removal via affinity chromatography after in-solution digestion. For on-column cleavage, the target protein can be directly released from fusion protein immobilized on resin.

Factors affecting the activity of recombinant TEV protease:

1) PMSF and AEBSF (1 mM), TLCK (1 mM), Bestatin (1 mg/mL), Pepstatin A (1 mM), EDTA (1 mM) and E-64 (3 mg/mL) show no inhibitory effect on rTEV activity;

2) Zinc ions (>5 mM) inhibit rTEV activity;

3) Cysteine-reactive reagents are potential inhibitors of rTEV.

Storage Conditions

Store at -20℃; shipped at -20 ~ 0℃. Valid for 24 months. For long-term preservation, storage at -80℃ is recommended. ▲ Avoid repeated freeze-thaw cycles.