ProTEV Plus

ProTEV Plus is an improved 48kDa version of the Nla protease from tobacco etch virus (TEV) that has been engineered to be more stable than native TEV protease for prolonged enzymatic activity. It is a highly specific proteolytic enzyme that cleaves within a seven-amino-acid sequence (ENLYFQ(G/S)). ProTEV Plus is active over a wide range of pH values (5.5–8.5) and temperatures (4–30°C). It can be used to cleave protein fusions that have been engineered with the above amino acid sequence at the desired cleavage site. The enzyme is compatible for both in-solution and on-column cleavage reactions...

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ProTEV Plus is an improved 48kDa version of the Nla protease from tobacco etch virus (TEV) that has been engineered to be more stable than native TEV protease for prolonged enzymatic activity. It is a highly specific proteolytic enzyme that cleaves within a seven-amino-acid sequence (ENLYFQ(G/S)). ProTEV Plus is active over a wide range of pH values (5.5–8.5) and temperatures (4–30°C). It can be used to cleave protein fusions that have been engineered with the above amino acid sequence at the desired cleavage site. The enzyme is compatible for both in-solution and on-column cleavage reactions. ProTEV Plus also contains an HQ tag (analogous to His tag) located at the N-terminus of the protein, which allows it to be immobilized on Ni-based affinity resins and removed from the cleavage reaction.

Learn more about our custom options for this product at: www.promega.com/myway/

Features - Benefits

• Active Over a Wide Range of pH and Temperatures: Cleave individual fusion proteins using optimal conditions to maintain activity and correct conformation.
• HQ-Tagged: Convenient removal of ProTEV Plus using Ni-based affinity resins after cleavage.
• Specific: Highly specific and active for its seven-amino acid sequence with minimal off-target effects.
• Cleaves Fusion Proteins Directly in Solution or Immobilized on Affinity Resins: ProTEV Plus is easy to use in multiple experimental formats.

Applications

• Cleavage of affinity tags from fusion proteins after protein purification.
• Removal of HaloTag® protein during protein purification/expression of fused proteins of interest.

References

1. Du, Y., Cai, Y., Hou, S. and Xu, X. (2012) Identification of the hetR recognition sequence upstream of hetZ in Anabaena sp. strain PCC 7120. J. Bacteriol. 194, 2297–2306.
2. Gong, Y.U.T. et al. (2012) Phase transitions in biogenic amorphous calcium carbonate. Proc. Natl. Acad. Sci. USA 109, 6088–93.
3. Morrow, B.J. et al. (2011) Antistaphylococcal activities of the new fluoroquinolone JNJ-Q2. Antimicrob. Agents Chemother. 55, 5512–21.
4. Ruepp, M.-D. et al. (2010) The 68 kDa subunit of mammalian cleavage factor I interacts with the U7 small nuclear ribonucleoprotein and participates in 3´-end processing of animal histone mRNAs. Nucleic Acids Res. 38, 7637–50.
5. Chen, Y.-C. et al. (2010) Protein arginine methylation facilitates cotranscriptional recruitment of pre-mRNA splicing factors. Mol. Cell. Biol. 30, 5245–56.

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