TEV Protease
Cat. No. | E027 | ||||||||
Name | TEV Protease | ||||||||
Unit | 100 μl | ||||||||
Category | Molecular Biology Enzymes and Kits | ||||||||
Description |
abm’s TEV Protease is an enhanced version of the site-specific protease derived from Tobacco Etch Virus (TEV). This optimized enzyme offers superior activity, stability, and site-specificity compared to the native form. TEV Protease cleaves fusion proteins with high precision at the Gln-Gly or Gln-Ser bond within the seven-amino acid recognition sequence Glu-Asn-Leu-Tyr-Phe-Gln-Gly/Ser (ENLYFQ(G/S)). The enzyme is highly effective across a broad range of temperatures (4–30°C, with an optimum at 30°C) and pH values (5.5–9.0), enabling flexible experimental conditions. Under optimal conditions, up to 99% cleavage can be achieved in just 1–2 hours. Additionally, the inclusion of a 6X-His tag at the N-terminus allows for convenient removal of TEV Protease post-cleavage using Ni-IDA Agarose Beads (Cat. No. G250) via affinity chromatography.
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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? | |
Yes, our TEV Protease (E027) contains a His tag.
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What is the molecular weight of this product? | |
The full molecular weight of E027 is around 28kDa.
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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.
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What buffer is the enzyme supplied with? | |
Enzyme supplied with 20X Reaction Buffer.
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What is the source of this enzyme? | |
The enzyme is produced recombinantly in E. coli, which has been engineered to express the enzyme gene. While the original gene may come from another organism, all production and purification occur using E. coli under controlled conditions.
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Issaro, N., Kongkaew, A., Jittmittraphap, A., Leaungwutiwong, P., Nimlamool, W., & Takuathung, M. N. (2023). Expression of polyprotein and 3D polymerase protein in Sf9 cells and immunogenicity against enterovirus A71B5 (Thailand strain). Journal of Applied Pharmaceutical Science, 13(9), 027-036. https://dx.doi.org/10.7324/JAPS.2023.93192
Liu, H., Yamaguchi, H., Kikkawa, M., & Shima, T. (2024). Heterogeneous local structures of the microtubule lattice revealed by cryo-ET and non-averaging analysis. bioRxiv, 2024-04. https://doi.org/10.1101/2024.04.30.591984
Mori, S., Nagae, M., & Yamasaki, S. (2024). Crystal structure of the complex of CLEC12A and an antibody that interferes with binding of diverse ligands. International Immunology, 36(6), 279-290. https://doi.org/10.1093/intimm/dxae006
Ogasawara, S., & Yamada, A. (2022). RNA editing with viral RNA-dependent RNA polymerase. ACS Synthetic Biology, 11(1), 46-52. https://doi.org/10.1021/acssynbio.1c00332
Takagi, M., Nagatani, A., Kawano, K., Hata, A., Yokoyama, A., Hayashida, K., ... & Matsuzaki, K. (2024). Stable and Minimum Size Solubilization of Membrane Proteins with Cocktails of Phospholipid Analogues. ACS Applied Materials & Interfaces, 16(46), 63358-63367. https://doi.org/10.1021/acsami.4c15697
Takahasi, K., Onomoto, K., Horiuchi, M., Kato, H., Fujita, T., & Yoneyama, M. (2019). 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. https://doi.org/10.1016/j.bbrc.2019.07.099
Tobita, Y., Hirano, K., Miura, D., Hatano, Y., Tsugawa, W., Ikebukuro, K., ... & Asano, R. (2025). A Versatile Method to Create Antibody/Split‐Enzyme Complexes and Its Application to a Rapid, Homogeneous, and Universal Electrochemical Immunosensing System. Advanced Sensor Research, 4(1), 2400112. https://doi.org/10.1002/adsr.202400112