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XPC Protein (AA 496-734) (His tag)

XPC Origine: Humain Hôte: Escherichia coli (E. coli) Recombinant > 90 % SDS
N° du produit ABIN5710632
  • Antigène Voir toutes XPC Protéines
    XPC (Xeroderma Pigmentosum, Complementation Group C (XPC))
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 496-734
    Origine
    • 4
    • 2
    • 2
    Humain
    Source
    • 6
    • 1
    • 1
    Escherichia coli (E. coli)
    Purification/Conjugué
    Cette XPC protéine est marqué à la His tag.
    Application
    SDS-PAGE (SDS)
    Séquence
    SLPAASSSSS SSKRGKKMCS DGEKAEKRSI AGIDQWLEVF CEQEEKWVCV DCVHGVVGQP LTCYKYATKP MTYVVGIDSD GWVRDVTQRY DPVWMTVTRK CRVDAEWWAE TLRPYQSPFM DREKKEDLEF QAKHMDQPLP TAIGLYKNHP LYALKRHLLK YEAIYPETAA ILGYCRGEAV YSRDCVHTLH SRDTWLKKAR VVRLGEVPYK MVKGFSNRAR KARLAEPQLR EENDLGLFG
    Purification
    SDS-PAGE
    Pureté
    > 90 %
    Top Product
    Discover our top product XPC Protéine
  • Indications d'application
    Optimal working dilution should be determined by the investigator.
    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    0.1-2 mg/mL
    Buffer
    20 mM Tris-HCl based buffer, pH 8.0
    Stock
    -80 °C,4 °C,-20 °C
    Stockage commentaire
    Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Antigène
    XPC (Xeroderma Pigmentosum, Complementation Group C (XPC))
    Autre désignation
    XPC (XPC Produits)
    Synonymes
    RAD4 Protein, XP3 Protein, XPCC Protein, XPC complex subunit, DNA damage recognition and repair factor Protein, xeroderma pigmentosum, complementation group C Protein, XPC Protein, Xpc Protein
    Sujet
    Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER, it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
    Poids moléculaire
    31.6 kDa
    UniProt
    Q01831
    Pathways
    Signalisation p53, Réparation de l'ADN
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