TEV Protease
| Cat. No. | E027 |
| Name | TEV Protease |
| Unit | 100 μl |
| Category | Molecular Biology Enzymes and Kits |
| Description |
abm’s TEV Protease is an improved version of the site-specific protease from Tobacco Etch Virus (TEV). abm’s TEV Protease has enhanced activity, stability and site-specificity when compared to the native enzyme. High specificity cleavage occurs between the Gln and Gly (or Ser) of the seven amino acid recognition sequence Glu-Asn-Leu-Tyr-Phe-Gln-Gly/Ser (ENLYFQ(G/S)) in the fusion protein of interest. TEV Protease is active over a wide range of temperatures (4 – 30°C; optimum 30°C) and pHs (5.5 – 9.0). At the optimal cleavage temperature for TEV Protease, 99% cleavage is often achieved in 1-2 hours. Owing to the presence of a 6X-His tag at the N-terminus, abm’s TEV Protease can be easily removed after the cleavage reaction by affinity chromatography with Ni-IDA Agarose Beads (Cat No. G250). |
| Application |
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| Concentration | 10U/ul |
| Material Citation | If use of this material results in a scientific publication, please cite the material in the following manner: Applied Biological Materials Inc, Cat. No. E027 |
| Does this enzyme contain a tag? | |
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Yes, our TEV Protease (E027) contains a His tag.
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| What is the molecular weight of this product? | |
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The full molecular weight of E027 is around 28kDa.
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| What is an Enzyme Unit defined as? | |
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One unit is defined as the amount of TEV Protease that is required to cleave >90% of 3 µg of control substrate in a 30 µl reaction for 1 hour at 30°C in 1X TEV Protease Reaction Buffer supplemented with 1 mM DTT.
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| What buffer is the enzyme supplied with? | |
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Enzyme supplied with 20X Reaction Buffer.
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- Liu, Y., Liu, Z., Tang, H., Shen, Y., Gong, Z., Xie, N., ... & Fu, Y. "The N 6-methyladenosine (m6A)-forming enzyme METTL3 facilitates M1 macrophage polarization through the methylation of STAT1 mRNA" American Journal of Physiology-Cell Physiology 317(4):C762-C775 (2019).
- Takahasi, K., Onomoto, K., Horiuchi, M., Kato, H., Fujita, T., & Yoneyama, M. "Identification of a new autoinhibitory domain of interferon-beta promoter stimulator-1 (IPS-1) for the tight regulation of oligomerization-driven signal activation" Biochemical and Biophysical Research Communications 517(4):662-669 (2019).