|Application ||WB, IHC-P, IHC-F, IF, E, IP|
|Calculated MW||113084 Da|
|Purification||Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant.|
|Shelf Life||18 months from date of despatch.|
|Other Names||Poly [ADP-ribose] polymerase 1, PARP-1, 220.127.116.11, ADP-ribosyltransferase diphtheria toxin-like 1, ARTD1, NAD(+) ADP-ribosyltransferase 1, ADPRT 1, Poly[ADP-ribose] synthase 1, PARP1, ADPRT, PPOL|
|Target/Specificity||Mouse anti-poly (ADP-ribose) polymerase 1 antibody, clone A6.4.12 recognizes poly (ADP-ribose) polymerase 1 (PARP-1), a ~116kD nuclear enzyme cleaved during apoptosis (Soldaniet al.2002). PARP-1, a caretaker enzyme, is involved in DNA damage repair (Langelieret al.2013), plays roles in diabetes pathophysiology (Andreoneet al.2012) and tumour proliferation (Rosadoet al2013.).As well as protecting cells from genomic instability, PARP-1 is involved in the development of both inflammatory and immune responses, and cell death by apoptosis and necrosis (Erdélyiet al.2005).Mouse anti-poly(ADP-ribose) polymerase 1 antibody, clone A6.4.12, targets PARP-1, an enzyme which represents a promising target for new developments in therapeutic treatment of immune mediated diseases (Rosadoet al.2013). PARP-1 has considerable potential for delivering selective tumour cell killing while sparing normal cells (Pintonet al.2013).|
|Preservative & Stabilisers||0.09% Sodium Azide|
|Storage||Store at +4℃ or at -20 ℃.|
|Precautions||Anti-Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 is for research use only and not for use in diagnostic or therapeutic procedures.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
1. Harris, J.L. et al. (2009) Aprataxin, poly-ADP ribose polymerase 1 (PARP-1) and apurinic endonuclease 1 (APE1) function together to protect the genome against oxidative damage. Hum Mol Genet. 18: 4102-17. 2. Freire, R. et al. (2001) Cleavage of the Bloom's syndrome gene product during apoptosis by caspase-3 results in an impaired interaction with topoisomerase IIIalpha.Nucleic Acids Res. 29 (15): 3172-80. 3. Krohn, A.J. et al. (1998) Staurosporine-induced apoptosis of cultured rat hippocampal neurons involves caspase-1-like proteases as upstream initiators and increased production of superoxide as a main downstream effector.J Neurosci. 18 (20): 8186-97. 4. Staples, C.J. et al. (2010) Cross-talk between the p38alpha and JNK MAPK pathways mediated by MAP kinase phosphatase-1 determines cellular sensitivity to UV radiation.J Biol Chem. 285 (34): 25928-40. 5. Alexander, B.M. et al. (2010) DNA repair protein biomarkers associated with time to recurrence in triple-negative breast cancer.Clin Cancer Res. 16: 5796-804. 6. Gueven, N. et al. (2004) Aprataxin, a novel protein that protects against genotoxic stress.Hum Mol Genet. 1081-93. 7. Gueven, N. et al. (2006) Defective p53 response and apoptosis associated with an ataxia-telangiectasia-like phenotype.Cancer Res. 66: 2907-12. 8. Kim, J.W. et al. (2000) Inhibition of homodimerization of poly(ADP-ribose) polymerase by its C-terminal cleavage products produced during apoptosis.J Biol Chem. 275: 8121-5. 9. Staples, C.J. et al. (2010) Cross-talk between the p38alpha and JNK MAPK pathways mediated by MAP kinase phosphatase-1 determines cellular sensitivity to UV radiation.J Biol Chem. 285: 25928-40. 10. Olaussen, K.A. et al. (2013) PARP1 impact on DNA repair of platinum adducts: Preclinical and clinical read-outs.Lung Cancer. 80: 216-22. 11. Fabrice, A.
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