Anti-PARP1 (cleaved form) Antibody

Poly [ADP-ribose] polymerase 1 (UniProt: P09874; also known as EC: 2.4.2.30, PARP-1, ADP-ribosyltransferase diphtheria toxin-like 1, ARTD1, NAD(+) ADP-ribosyltransferase 1, ADPRT 1, Poly[ADP-ribose] synthase 1) is encoded by the PARP1 (also known as ADPRT, PPOL) gene (Gene ID: 142) in human. PARP1 is zinc-dependent DNA binding protein that recognizes DNA strand breaks and is presumed to play a role in DNA repair. It is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Its DNA-binding region is localized to amino acids 2-372. PARP1 contains two zinc-finger regions (aa 9-93 and 113-203). PARP is cleaved between amino acids Asp214 and Gly215 to yield two fragments: a 29 kDa (N-terminal) and a 85 kDa (C-terminal DNA-binding domain). The carboxyl-terminally located 54-kDa domain of PARP represents the NAD1-binding domain with the characteristic “PARP signature,” which includes a highly conserved sequence comprising the catalytically crucial amino acid residue Glu-988. Its catalytic activity is stimulated by noncovalent contact of the DNA-binding domain with DNA strand breaks and results in the post-translational modification of various acceptor proteins. In between the DNA binding domain and the NAD1-binding domain, it also contains a 22-kDa automodification domain. (Ref.: Alvarez-Gonzalez, R., et al. (1999). J. Biol. Chem. 274(45); 32122–32126).

~89 kDa observed

Epitope: DNA binding domain

KLH-conjugated linear peptide corresponding to the DNA binding domain of human PARP1.

Immunocytochemistry Analysis: A 1:500 dilution from a representative lot detected cleaved PARP1 in staurosporine-untreated and staurosporine-treated HeLa cells.

This Anti-PARP1 (cleaved form) Antibody is validated for use in WB, IC for the detection of PARP1 (cleaved form).

Other homologies: Rat and Mouse (90% sequence homology).

This antibody recognizes cleaved PARP1 at the DNA binding domain.

Control
Jurkat cell lysate untreated and Camptothecin-treated

Evaluated by Western Blot in Jurkat cell lysate, untreated and Camptothecin-treated.

Western Blot Analysis: A 1:50,000 dilution of this antibody detected cleaved PARP1 in 10 µg of Jurkat cell lysate, untreated and Camptothecin-treated.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Replaces: 04-576