TEV Protease

E027100 μl

Customize TEV Protease
1 x TEV Protease   + $0.00
1 x 20X TEV Rxn Buffer   + $0.00
1 x 100mM DTT   + $0.00

* Required Fields

Your Customization
TEV Protease
TEV Protease

In stock




    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).

    • Cleavage of tags from recombinant fusion proteins containing a TEV recognition site
    • One step affinity removal of His-tagged TEV after cleavage
    Unit quantity100 μl

    Supporting Protocol




          Does this enzyme contain a tag?
          Yes, our TEV Protease (E027) contains a His tag.
          What is the molecular weight of this product?
          The full molecular weight of E027 is around 28kDa.
          What is an Enzyme Unit defined as?
          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.
          What buffer is the enzyme supplied with?
          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).