| Cat# | DIA-573 |
| Description | A genetically engineered TEV protease expressed in E. coli with a His-tag (6× His) and purified. It retains the native TEV enzyme activity while exhibiting enhanced stability and specificity over a broad temperature range. Used to cleave affinity tags from fusion proteins. |
| Form | Liquid |
| Unit Definition | One unit of rTEV protease activity is defined as the amount of enzyme required to cleave over 85% of 3 µg of substrate protein in 1 hour at 30 °C in 1× rTEV buffer (50 mM Tris-HCl, pH 8.0, 0.1 mM EDTA, 1 mM DTT). |
| Synonyms | Recombinant TEV protease |
| Buffer | 25 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, 5mM DTT, 50% (v/v) Glycerol, pH 8.0 |
| Applications | Cleavage of affinity tags from fusion proteins. |
| Product Overview | Recognizes the seven-amino-acid sequence EXXYXQ↓(G/S), commonly Glu-Asn-Leu-Tyr-Phe-Gln↓-Gly. Optimal activity at pH 7.0 and 30 °C, but retains activity from pH 6.0–8.5 and 4–30 °C, allowing flexible reaction conditions. Post-cleavage, the N-terminal 6× His-tag enables removal via Ni-NTA resin for efficient target protein purification. |
| Purity | ≥95% (SDS-PAGE) |
| Package | 1/5/10 KU |
| Download Datasheet: |  |
