|Species||Tobacco etch virus|
|Purity||>95% by SDS PAGE|
TEV protease is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV). It is a member of chymotrypsin-like proteases. Due to its high sequence specificity it is frequently used for the cleavage of fusion proteins and removal of tags from recombinant proteins in vitro and in vivo.
This recombinant TEV protease is genetically improved 28 kDa version of the Nla protease from tobacco etch virus (TEV) that has been engineered to be more stable than native TEV protease with higher enzymatic activity. It contains His6 tag located at the N-terminus of the protein, which allows it to be immobilized on Ni-based affinity resins and removed from the cleavage reaction. It is active over a wide range of pH values (4-8.5) and temperatures (4-34°C). The preferred recognition sequence is ENLYFQ|S(G,A), but it cleaves also motives EXLYFQ|S(G,A), where X could be any amino acid residue (in parenthesis are alternative residues).
Cleavage of affinity tags from fusion proteins after protein purification. Cleaves fusion proteins directly in solution or immobilized on affinity resins.
50mM Tris pH 7,5, 1 mM EDTA, 5 mM DTT , 40% glycerol
Highly specific and active for its seven-amino acid sequence with minimal off-target effects. Activity more than 10,000 units per 1 mg protein. The activity depends on the type of target protein. The optimal amount of enzyme should be tested for each target protein.
-20°C, do not store at -80°C
For research use only. Not for use in diagnostic procedures.