| Source: |
Escherichia coli |
| Purity: |
> 90% by SDS-PAGE analysis. |
| Physical Appearance: |
Clear colorless liquid. |
| Formulation: |
A 0.2 µm filtered solution in 25 mM Tris-HCl, pH8.0, 75 mM NaCl, 5 mM EDTA, 10 mM GSH, with 50 % glycerol. |
| Stability & Storage: |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70°C as supplied.- 3 months, -20 to -70°C under sterile conditions after opening. |
| Synonyms: |
P1 Protease |
| Background: |
The TEV protease, derived from the tobacco etch virus, is a catalytic component of the Nuclear Inclusion a (NIa) protein. It consists of 241 amino acids, yielding a molecular weight of 27 kDa. TEV protease recognizes a specific amino acid sequence, typically E-X-X-Y-X-Q (or S)/X', where it cleaves between Q (or S)/X'. Here, X and X' can denote any amino acid except for X', which cannot be P. The preferred cleavage site for TEV protease is ENLYFQ/G.
TEV protease exhibits remarkable versatility due to its high specificity and robust performance under varied conditions such as broad pH ranges and ionic strengths. Compared to other proteases like EK and thrombin commonly used in biochemical applications, particularly in recombinant protein production, TEV protease is highly favored. Its optimal cleavage temperature is 30°C, although it remains active at temperatures as low as 4°C. After digestion, TEV protease can be conveniently removed from the reaction using Ni2+-chelate affinity chromatography targeting the His tag sequence. |
