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TEV Protease Protein

Spezies: Tobacco Etch Virus (TEV) Wirt: Escherichia coli (E. coli) Recombinant > 95 % by SDS-PAGE analyses.
Produktnummer ABIN2018393
  • Target
    TEV Protease
    Protein-Typ
    Recombinant
    Spezies
    Tobacco Etch Virus (TEV)
    Quelle
    • 1
    Escherichia coli (E. coli)
    Produktmerkmale
    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.
    Reinheit
    > 95 % by SDS-PAGE analyses.
    Sterilität
    Sterile
  • Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Buffer
    Sterile liquid solution contains 50 mM Tris, 5 mM DTT, 50 % glycerol, pH 7.5.
    Handhabung
    Avoid freeze-thaw cycles.
    Lagerung
    -20 °C
    Informationen zur Lagerung
    Recombinant Tobacco Etch Virus Protease (rTEV) remains stable up to 1 year at -20 °C from date of receipt.
    Haltbarkeit
    12 months
  • Target
    TEV Protease
    Substanzklasse
    Viral Protein
    Hintergrund
    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
    Molekulargewicht
    28.4 kDa, observed by reducing SDS-PAGE.
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