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PARP2 Protein

PARP2 Spezies: Maus Wirt: Insect cells (Sf9) Recombinant 98 % (SDS-PAGE).
Produktnummer ABIN925019
  • Target Alle PARP2 Proteine anzeigen
    PARP2 (Poly (ADP-Ribose) Polymerase 2 (PARP2))
    Protein-Typ
    Recombinant
    Spezies
    • 5
    • 2
    Maus
    Quelle
    • 3
    • 2
    • 1
    • 1
    Insect cells (Sf9)
    Produktmerkmale
    380 units/mg (one unit synthesizes 1 nmole of poly(ADP-ribose) per min at 25°C, pH 7.5.
    Aufreinigung
    Affinity purified
    Reinheit
    98 % (SDS-PAGE).
    Top Product
    Discover our top product PARP2 Protein
  • Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Lagerung
    -80 °C
  • Target
    PARP2 (Poly (ADP-Ribose) Polymerase 2 (PARP2))
    Andere Bezeichnung
    PARP-2 (PARP2 Produkte)
    Synonyme
    ADPRT2 Protein, ADPRTL2 Protein, ADPRTL3 Protein, ARTD2 Protein, PARP-2 Protein, pADPRT-2 Protein, Adprt2 Protein, Adprtl2 Protein, Aspartl2 Protein, C78626 Protein, cb996 Protein, adprtl2 Protein, ADPRT-2 Protein, APP Protein, ATPARP1 Protein, PARP1 Protein, POLY(ADP-RIBOSE) POLYMERASE Protein, POLY(ADP-RIBOSE) POLYMERASE 1 Protein, PP Protein, T14P8.19 Protein, T14P8_19 Protein, poly(ADP-ribose) polymerase Protein, poly(ADP-ribose) polymerase 2 Protein, poly(ADP-ribose) polymerase 2 Protein, poly (ADP-ribose) polymerase family, member 2 Protein, poly (ADP-ribose) polymerase 2 Protein, poly(ADP-ribose) polymerase 2 S homeolog Protein, poly(ADP-ribose) polymerase Protein, PARP2 Protein, Parp2 Protein, parp2 Protein, parp2.S Protein
    Hintergrund
    The cDNA encoding human poly(ADP-ribose) polymerase (PARP) was cloned by several groups simultaneously. With the discovery of new members (homologs) of the PARP family, PARP is newly referred to as PARP-1. The isolated cDNAs from mouse and human encode a protein with considerable homology to the catalytic domain of PARP-1. This protein, termed PARP-2, is a 64 kDa protein that contains a nuclear localization signal (NLS) and is activated by DNA breaks, although its DNA- binding domain is very different from that of PARP-1. In recent years evidence has accumulated that poly(ADP-ribose) polymerase (PARP) plays a role in DNA repair and a substantial effort has been invested to elucidate the physiological function of the PARP pathway in cellular recovery from DNA damage. PARP has been found in the base excision repair (BER) complex with DNA polymerase-, ligase III and x-ray repair cross-complementing 1 (XRCC1). PARP- 1 and PARP-2, even though lacking the zinc- finger domains, bind to single and double strand breaks during oxidative stress. In general, it appears that an early enzymatic activation of PARP occurs upon DNA-strand break formation. Binding of PARP to a DNA nick may then cause a transient halt to cellular activity and protect the DNA from sister chromatid associated proteins such as histones. Nicotinamide is cleaved in this step from the substrate NAD+ by PARP and the so synthesized poly(ADP)-ribose (PAR) is then used to generate ATP. Specific
    Pathways
    DNA Reparatur
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