TEV Protease

Description:
TEV (Tobacco Etch Virus) Protease is a highly site-specific cysteine protease that recognizes the cleavage site of Glu-Asn-Leu-Tyr-Phe-Gln-Gly and cleaves between Gln and Gly. TEV protease is a very useful enzyme for cleaving fusion proteins due to its high specificity and its high activity rate. TEV Protease contains an N-terminal His-tag, and it can be removed by Ni-NTA column after cleavage reaction.

Application:
- Removal of fusion tags from recombinant proteins
- Highly dynamic and precise cleavage capabilities
- purification of proteins and peptides

Supplied With:
TEV substrate, 100 µl
10X TEV buffer

Source:
E. coli derived from Tobacco Etch Virus.

Label: His-tag

Reaction Conditions:
TEV protease is maximally active at 34°C, but its recommended to perform digests at room temperature (20°C) or 4°C. The activity of TEV protease is approximately 3-fold greater at 20°C than at 4°C.

10X TEV buffer
50 mM Tris-HCl, 150 mM NaCl, pH 8.0

Recommended Storage Condition: -20°C

Figures:

Figure 1

Figure 2, 69.8 kDa TEV substrate protein is incubated with TurboTEV. The cleaved products are 41.2 kDa and 27.7 kDa, respectively.