TEV Protease is a restriction grade protease that has robust activity at 4°C with high specificity and great stability. The optimal temperature for cleavage with this enzyme is 34°C. The protease is used for the removal of affinity tags from fusion proteins. The structure of TEV protease is similar to that of the serine protease family. Like serine proteases, TEV protease utilizes a catalytic triad of residues to hydrolyze peptide bonds. The distinguishing feature of TEV protease, however, is that instead of the serine nucleophile in the triad Ser-Asp-His, there is a cysteine, which may explain the resistance of TEV protease to protease inhibitors which are commonly used.
Type: Primary
Antigen: TEV Protease
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: All