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ProTEV Plus

Engineered Protease with Greater Stability, Prolonged Activity Over Native TEV Protease

  • Active over broad pH (5.5–8.5) and temperature (4–30°C) range
  • Cleaves protein fusions with the ENLYFQ(G/S) sequence
  • Use with in-solution and on-column digestions
  • Supplied at a concentration of 5u/μl

Size

Catalog number selected: V6101

$ 138.00 Your price: Log In

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ProTEV Plus
1,000u
$ 138.00
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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/custom/


  • 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.
11338TA.eps
Cleavage of 20µg of GST-MBP fusion protein with ProTEV protease after 60 minutes at 30°C.

Specifications

You are viewing: V6101 Change Configuration

What's in the box?

Item Part # SizeConcentrationAvailable Separately

DTT

P117B 1 × 250μl100mM View Product

ProTEV Buffer, 20X

V602A 1 × 1ml

ProTEV Plus

V610A 1 × 1,000u5u/μl

SDS

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Certificate of Analysis

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Use Restrictions

For Research Use Only. Not for Use in Diagnostic Procedures.

Storage Conditions

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Specifications

You are viewing: V6102 Change Configuration

What's in the box?

Item Part # SizeConcentrationAvailable Separately

DTT

P117C 1 × 1.25ml100mM View Product

ProTEV Buffer, 20X

V602B 1 × 8ml

ProTEV Plus

V610B 1 × 8,000u5u/μl

SDS

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Certificate of Analysis

Search for Specific Certificate:

View more results
View more results
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Use Restrictions

For Research Use Only. Not for Use in Diagnostic Procedures.

Storage Conditions

BB
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