Poly(ADP-Ribose) Polymerase-1 antibody | A6.4.12
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Mouse anti Poly(ADP-Ribose) Polymerase-1
- Product Type
- Monoclonal Antibody
- Poly(ADP-Ribose) Polymerase-1
|Mouse anti poly (ADP-ribose) polymerase 1 antibody, clone A6.4.12 recognizes poly (ADP-ribose) polymerase 1 (PARP-1), a ~116 kDa nuclear enzyme, cleaved during apoptosis (Soldani et al. 2002).
PARP-1, a caretaker enzyme, is involved in DNA damage repair (Langelier et al. 2013), plays roles in diabetes pathophysiology (Andreone et al. 2012) and tumour proliferation (
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 (Erdélyi et 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 (
- Target Species
- Species Cross-Reactivity
Target Species Cross Reactivity Hamster Mouse Drosophila Xenopus Rat
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.09% sodium azide (NaN3)
- Carrier Free
- Human PARP-1
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells from immunized BALB/c mice were fused with cells of mouse NS0 myeloma cell line.
- For research purposes only
- 12 months from date of despatch
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Frozen|
|Immunohistology - Paraffin 1|
- 1 Clone A6.4.12 requires antigen retrieval using heat treatment prior to staining of paraffin sections. Sodium citrate buffer pH 6.0 is recommended for this purpose.
References for Poly(ADP-Ribose) Polymerase-1 antibody
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.
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.
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.
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.
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.
Gueven, N. et al. (2004) Aprataxin, a novel protein that protects against genotoxic stress.
Hum Mol Genet. 13 (10): 1081-93.
Gueven, N. et al. (2006) Defective p53 response and apoptosis associated with an ataxia-telangiectasia-like phenotype.
Cancer Res. 66: 2907-12.
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.
View The Latest Product References
Hanzlikova, H. et al. (2017) Overlapping roles for PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin.
Nucleic Acids Res. 45 (5): 2546-2557.
Olaussen, K.A. et al. (2013) PARP1 impact on DNA repair of platinum adducts: Preclinical and clinical read-outs.
Lung Cancer. 80: 216-22.
et al. (2012) PARP and adjuvant cisplatin-based chemotherapy in non-small-cell lung cancer.
US patent: 20120277110
Geistrikh, I. et al. (2011) Ca2+-induced PARP-1 activation and ANF expression are coupled events in cardiomyocytes.
Biochem J. 438: 337-47.
Mirzaa, G.M. et al. (2014) Mutations in CENPE define a novel kinetochore-centromeric mechanism for microcephalic primordial dwarfism.
Hum Genet. 133: 1023-39.
Milner, R. et al. (2013) Validation of the BRCA1 antibody MS110 and the utility of BRCA1 as a patient selection biomarker in immunohistochemical analysis of breast and ovarian tumours.
Virchows Arch. 462: 269-79.
Inbar, D. et al. (2012) Erythropoietin-driven signalling and cell migration mediated by polyADP-ribosylation.
Br J Cancer. 107: 1317-26.
Buchsbaum, S. et al. (2012) FAT10 is a proteasomal degradation signal that is itself regulated by ubiquitination.
Mol Biol Cell. 23: 225-32.
Mullane, S.A. et al. (2016) Expression Levels of DNA Damage Repair Proteins Are Associated With Overall Survival in Platinum-Treated Advanced Urothelial Carcinoma.
Clin Genitourin Cancer. 14 (4): 352-9.
Zeng, J. et al. (2016) Nucleolar PARP-1 Expression Is Decreased in Alzheimer's Disease: Consequences for Epigenetic Regulation of rDNA and Cognition.
Neural Plast. 2016: 8987928.
Okuda, A. et al. (2017) Poly(ADP-ribose) polymerase inhibitors activate the p53 signaling pathway in neural stem/progenitor cells.
BMC Neurosci. 18 (1): 14.
Kubelac, P. et al. (2020) Changes in DNA Damage Response Markers with Treatment in Advanced Ovarian Cancer.
Cancers (Basel). 12(3): 707.
Komulainen, E. et al. (2021) Parp1 hyperactivity couples DNA breaks to aberrant neuronal calcium signalling and lethal seizures.
EMBO Rep. 22 (5): e51851.
Pinton, G. et al. (2013) PARP1 inhibition affects pleural mesothelioma cell viability and uncouples AKT/mTOR axis via SIRT1.
J Cell Mol Med. 17: 233-41.
Rosado, M. et al. (2013) Beyond dna repair,the immunological role of parp-1 and its siblings.
Immunology. 139: 428-37.
Andreone, T. et al. (2012) Cytokine-mediatedβ-cell damage in PARP-1-deficient islets.
Am J Physiol Endocrinol Metab. 303: E172-9.
Langelier, M.F. and Pascal, J.M. (2013) PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis.
Curr Opin Struct Biol. 23: 134-43.
- Entrez Gene
- GO Terms
- GO:0003677 DNA binding
- GO:0003950 NAD+ ADP-ribosyltransferase activity
- GO:0005635 nuclear envelope
- GO:0005667 transcription factor complex
- GO:0005730 nucleolus
- GO:0006366 transcription from RNA polymerase II promoter
- GO:0006471 protein ADP-ribosylation
- GO:0008134 transcription factor binding
- GO:0008270 zinc ion binding
- View More GO Terms
- GO:0042802 identical protein binding
- GO:0032869 cellular response to insulin stimulus
- GO:0045449 regulation of transcription
- GO:0047485 protein N-terminus binding
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