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TEV Protease Protéine

Cette protéine Recombinant est produite dans Escherichia coli (E. coli).
N° du produit ABIN2018393

Aperçu rapide pour TEV Protease Protéine (ABIN2018393)

Antigène

TEV Protease

Type de proteíne

Recombinant

Origine

Tobacco Etch Virus (TEV)

Source

  • 1
Escherichia coli (E. coli)

Pureté

> 95 % by SDS-PAGE analyses.
  • Attributs du produit

    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.

    Stérilité

    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.

    Conseil sur la manipulation

    Avoid freeze-thaw cycles.

    Stock

    -20 °C

    Stockage commentaire

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

    Date de péremption

    12 months
  • Antigène

    TEV Protease

    Classe de substances

    Viral Protein

    Sujet

    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

    Poids moléculaire

    28.4 kDa, observed by reducing SDS-PAGE.
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