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TEV Protease Protein

This Recombinant TEV Protease protein is produced in Escherichia coli (E. coli).
Catalog No. ABIN2018393
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$293.51
$345.31
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10000 IU
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Quick Overview for TEV Protease Protein (ABIN2018393)

Target

TEV Protease

Protein Type

Recombinant

Origin

Tobacco Etch Virus (TEV)

Source

  • 1
Escherichia coli (E. coli)

Purity

> 95 % by SDS-PAGE analyses.
  • Characteristics

    6 IU/μl
    Unit Definition: One unit of TEV protease cleaves > 85 % of 3 μg of control substrate in 1 hour at pH 8.0 at 30 °C.

    Sterility

    Sterile
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  • Restrictions

    For Research Use only
  • Format

    Liquid

    Buffer

    Sterile liquid solution contains 50 mM Tris, 5 mM DTT, 50 % glycerol, pH 7.5.

    Handling Advice

    Avoid freeze-thaw cycles.

    Storage

    -20 °C

    Storage Comment

    Recombinant Tobacco Etch Virus Protease (rTEV) remains stable up to 1 year at -20 °C from date of receipt.

    Expiry Date

    12 months
  • Target

    TEV Protease

    Target Type

    Viral Protein

    Background

    Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the Tobacco Etch Virus (TEV). The optimum recognition site for this enzyme is the sequence Glu-Asn-Leu-Tyr-Phe-Gln-(Gly/Ser) [ENLYFQ(G/S)] and cleavage occurs between the Gln and Gly/Ser residues, The most commonly used sequence is ENLYFQG. The protease is used to cleave affinity tags from fusion proteins. The optimal temperature for cleavage is 30 °C, also it can be used at temperature as low as 4 °C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin.Recombinant Tobacco Etch Virus Protease (rTEV) contains 231 amino acids with N-terminal His tagged. A fully biologically active molecule, rTEV has a molecular mass of 28.4 kDa and is obtained by proprietary chromatographic techniques.
    Synonyms: rTEV, TEV, P1 protease

    Molecular Weight

    28.4 kDa, observed by reducing SDS-PAGE.
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