Product Pathways - Apoptosis
PARP Antibody #9542
|W||H M R Mk||Endogenous||89, 116||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
PARP Antibody detects endogenous levels of full length PARP1 (116 kDa), as well as the large fragment (89 kDa) of PARP1 resulting from caspase cleavage. The antibody does not cross-react with related proteins or other PARP isoforms.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the caspase cleavage site in PARP. Antibodies are purified by protein A and peptide affinity chromatography.
PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).
- Satoh, M.S. and Lindahl, T. (1992) Nature 356, 356-358.
- Lazebnik, Y. A. et al. (1994) Nature 371, 346-347.
- Cohen, G.M. (1997) Biochem. J. 326, 1-16.
- Nicholson, D. W. et al. (1995) Nature 376, 37-43.
- Tewari, M. et al. (1995) Cell 81, 801-809.
- Oliver, F.J. et al. (1998) J. Biol. Chem. 273, 33533-33539.
- Li, J. et al. (2002) Microarray analysis reveals an antioxidant responsive element-driven gene set involved in conferring protection from an oxidative stress-induced apoptosis in IMR-32 cells. J. Biol. Chem. 277, 388-394. Applications: Western Blotting
- Cheong, J. W. et al. (2003) Induction of apoptosis by apicidin, a histone deacetylase inhibitor, via the activation of mitochondria-dependent caspase cascades in human Bcr-Abl-positive leukemia cells. Clin Cancer Res. 9 (13), 5018-27. Applications: Western Blotting
- Soldatenkov, V. A. et al. (2002) Transcriptional repression by binding of poly(ADP-ribose) polymerase to promoter sequences. J. Biol. Chem. 277, 665-670. Applications: IP
- Chandrasekar, B. et al. (2004) Activation of intrinsic and extrinsic proapoptotic signaling pathways in interleukin-18-mediated human cardiac endothelial cell death. J. Biol. Chem. 279, 20221-20233. Applications: Western Blotting
- Kumar-Sinha, C. et al. (2003) Transcriptome analysis of HER2 reveals a molecular connection to fatty acid synthesis. Cancer Res. 63, 132-139. Applications: Western Blotting
- Biton, S. and Ashkenazi, A. (2011) Cell 145, 92-103. Applications: Western Blotting
- Jak, M. et al. (2011) Blood 118, 5178-88. Applications: Western Blotting
- May, K.L. et al. (2010) Infect Immun 78, 4691-6. Applications: Western Blotting
- He, S. et al. (2009) Cell 137, 1100-11. Applications: Western Blotting
- Thome, C.H. et al. (2012) Mol Cell Proteomics , . Applications: Western Blotting
- Elzi, D.J. et al. (2012) Mol Cell Biol 32, 4388-99. Applications: Western Blotting
- Gupta, S. et al. (2013) PLoS Pathog 9, e1003272. Applications: Western Blotting
- Iden, S. et al. (2012) Cancer Cell 22, 389-403. Applications: Western Blotting
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For Research Use Only. Not For Use In Diagnostic Procedures.