Anti-PARP/PARP1 Antibody Picoband® Fluoro488 Conjugated

Poly [ADP-ribose] polymerase 1 (PARP1), also known as ADPRT or PPOL is an enzyme that in humans is encoded by the PARP1 gene. PARP1 gene is mapped to 1q42.12. This gene encodes a chromatin-associated enzyme, poly (ADP-ribosyl) transferase, which modifies various nuclear proteins by poly (ADP-ribosyl) ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, this enzyme may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes.

Poly [ADP-ribose] polymerase 1; PARP-1;2.4.2.30; ADP-ribosyltransferase diphtheria toxin-like 1; ARTD1; NAD (+) ADP-ribosyltransferase 1; ADPRT 1; Poly[ADP-ribose] synthase 1; PARP1; ADPRT, PPOL

E.coli-derived human PARP recombinant protein (Position: Q670-R858) . Human PARP shares 94% and 95% amino acid (aa) sequence identity with mouse and rat PARP, respectively.

Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain (at protein level) . Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa. .

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. Mediates the poly (ADP- ribosyl) ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to ly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. .

1. Ambrose, H. E., Willimott, S., Beswick, R. W., Dantzer, F., Menissier de Murcia, J., Yelamos, J., Wagner, S. D. Poly (ADP-ribose) polymerase-1 (Parp-1) -deficient mice demonstrate abnormal antibody responses. Immunology 127: 178-186, 2008. 2. Doege, C. A., Inoue, K., Yamashita, T., Rhee, D. B., Travis, S., Fujita, R., Guarnieri, P., Bhagat, G., Vanti, W. B., Shih, A., Levine, R. L., Nik, S., Chen, E. I., Abeliovich, A. Early-stage epigenetic modification during somatic cell reprogramming by Parp1 and Tet2. Nature 488: 652-655, 2012.