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TEV Protease Protein

This Recombinant protein is produced in Escherichia coli (E. coli).
Catalog No. ABIN2018393

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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