Lane 1: Jurkat cell lysate
Lane 2: A549 cell lysate
Recombinant Rabbit monoclonal primary
Cleaved PARP Recombinant Rabbit Monoclonal Antibody [SU0314] (ET1608-10)
Jurkat cell lysate, A549 cell lysate, Hela.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
ADP-ribosyltransferase diphtheria toxin-like 1 antibody; ADPRT 1 antibody; ADPRT antibody; ADPRT1 antibody; APOPAIN antibody; ARTD1 antibody; NAD(+) ADP-ribosyltransferase 1 antibody; PARP antibody; PARP-1 antibody; PARP1 antibody; PARP1_HUMAN antibody; Poly [ADP-ribose] polymerase 1 antibody; Poly ADP ribose polymerase 1 antibody; Poly[ADP-ribose] synthase 1 antibody; PPOL antibody; SCA1 antibody
Phosphorylated by PRKDC and TXK.; Poly-ADP-ribosylated on glutamate and aspartate residues by autocatalysis. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites. ADP-ribosylated on serine by autocatalysis; serine ADP-ribosylation takes place following interaction with HPF1.; S-nitrosylated, leading to inhibit transcription regulation activity.
Poly(ADP-ribose) polymerase-1 (PARP-1), also designated PARP, is a nuclear DNA-binding zinc finger protein that influences DNA repair, DNA replication, modulation of chromatin structure, and apoptosis. In response to genotoxic stress, PARP-1 catalyzes the transfer of ADP-ribose units from NAD(+) to a number of acceptor molecules including chromatin. PARP-1 recognizes DNA strand interruptions and can complex with RNA and negatively regulate transcription. Actinomycin D- and etoposide-dependent induction of caspases mediates cleavage of PARP-1 into a p89 fragment that traverses into the cytoplasm. Apoptosis-inducing factor (AIF) translocation from the mitochondria to the nucleus is PARP-1-dependent and is necessary for PARP-1-dependent cell death. PARP-1 deficiencies lead to chromosomal instability due to higher frequencies of chromosome fusions and aneuploidy, suggesting that poly(ADP-ribosyl)ation contributes to the efficient maintenance of genome integrity. This antibody recognizes the apoptosis-specific 89 kDa catalytic domain fragment, but it does not recognize the full-length PARP-1 or the 24 kDa DNA binding domain fragment.
Liu, Xia et al.
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