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TEV Protease

Cat. No.
E027
Unit
100 μl
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
  • Cleavage of tags from recombinant fusion proteins containing a TEV recognition site
  • One step affinity removal of His-tagged TEV after cleavage
Concentration 10U/ul
Search CoA here

The full molecular weight of E027 is around 28kDa.

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.

Enzyme supplied with 20X Reaction Buffer.

  • 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).

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