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MutM (AA 1-269) protein (His tag)

Spezies: E. coli Wirt: Escherichia coli (E. coli) Recombinant > 90% by SDS-PAGE SDS
Produktnummer ABIN1098227
  • Target
    MutM
    Protein-Typ
    Recombinant
    Proteineigenschaft
    AA 1-269
    Spezies
    E. coli
    Quelle
    • 1
    Escherichia coli (E. coli)
    Aufreinigungstag / Konjugat
    His tag
    Applikation
    SDS-PAGE (SDS)
    Sequenz
    MPELPEVETS RRGIEPHLVG ATILHAVVRN GRLRWPVSEE IYRLSDQPVL SVQRRAKYLL LELPEGWIII HLGMSGSLRI LPEELPPEKH DHVDLVMSNG KVLRYTDPRR FGAWLWTKEL EGHNVLTHLG PEPLSDDFNG EYLHQKCAKK KTAIKPWLMD NKLVVGVGNI YASESLFAAG IHPDRLASSL SLAECELLAR VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK GEPCRVCGTP IVATKHAQRA TFYCRQCQK
    Aufreinigung
    purified by chromatography
    Reinheit
    > 90% by SDS-PAGE
  • Applikationshinweise
    Optimal working dilution should be determined by the investigator.
    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Konzentration
    0.5 mg/mL
    Buffer
    20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol 0.1 M NaCl,1 MM DTT
    Lagerung
    4 °C,-20 °C,-80 °C
    Informationen zur Lagerung
    Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C. Avoid repeated freezing and thawing cycles.
  • Target
    MutM
    Hintergrund
    MutM, also known as formamidopyrimidine DNA glycosylase, is a base excision repair enzyme which recognizes and removes a wide range of oxidized purines from correspondingly damaged DNA. This protein is nonredundant and required to rapidly remove its substrate lesions on the chromosome. In addition, it also repaired a significant portion of the lesions recognized by Endo III, suggesting that it plays a prominent role in the global repair of both purine damage and pyrimidine damage in vivo. Recombinant E. coli mutM protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.
    Molekulargewicht
    32.4 kDa (289aa) confirmed by MALDI-TOF
    NCBI Accession
    NP_418092
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