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Poly(ADP-Ribose) Polymerase-1 antibody | A6.4.12

Mouse anti Poly(ADP-Ribose) Polymerase-1

Product Type
Monoclonal Antibody
Clone
A6.4.12
Isotype
IgG1
Specificity
Poly(ADP-Ribose) Polymerase-1

Product Code Applications Pack Size List Price Your Price Qty
MCA1522G
Datasheet Datasheet Datasheet
SDS Safety Datasheet SDS
C E IF IP P * WB 0.1 mg loader
List Price Your Price
loader

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 (Rosado et al 2013.).

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 (Rosado et al. 2013). PARP-1 has considerable potential for delivering selective tumour cell killing while sparing normal cells (Pinton et al. 2013).

Target Species
Human
Species Cross-Reactivity
Target SpeciesCross Reactivity
Hamster
Mouse
Drosophila
Xenopus
Rat
N.B. Antibody reactivity and working conditions may vary between species.
Product Form
Purified IgG - liquid
Preparation
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
Yes
Immunogen
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.
Regulatory
For research purposes only
Guarantee
12 months from date of despatch

This product is shipped at ambient temperature. It is recommended to aliquot and store at -20°C on receipt. When thawed, aliquot the sample as needed. Keep aliquots at 2-8°C for short term use (up to 4 weeks) and store the remaining aliquots at -20°C.

Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Application Name Verified Min Dilution Max Dilution
ELISA
Immunofluorescence
Immunohistology - Frozen
Immunohistology - Paraffin 1
Immunoprecipitation
Western Blotting 1/1000 1/5000
  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.
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.

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References for Poly(ADP-Ribose) Polymerase-1 antibody

  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. 13 (10): 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. View The Latest Product References
  10. 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.
  11. Olaussen, K.A. et al. (2013) PARP1 impact on DNA repair of platinum adducts: Preclinical and clinical read-outs.
    Lung Cancer. 80: 216-22.
  12. Fabrice, A. et al. (2012) PARP and adjuvant cisplatin-based chemotherapy in non-small-cell lung cancer.
    US patent: 20120277110
  13. Geistrikh, I. et al. (2011) Ca2+-induced PARP-1 activation and ANF expression are coupled events in cardiomyocytes.
    Biochem J. 438: 337-47.
  14. Mirzaa, G.M. et al. (2014) Mutations in CENPE define a novel kinetochore-centromeric mechanism for microcephalic primordial dwarfism.
    Hum Genet. 133: 1023-39.
  15. 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.
  16. Inbar, D. et al. (2012) Erythropoietin-driven signalling and cell migration mediated by polyADP-ribosylation.
    Br J Cancer. 107: 1317-26.
  17. Buchsbaum, S. et al. (2012) FAT10 is a proteasomal degradation signal that is itself regulated by ubiquitination.
    Mol Biol Cell. 23: 225-32.
  18. 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.
  19. 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.
  20. 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.
  21. Kubelac, P. et al. (2020) Changes in DNA Damage Response Markers with Treatment in Advanced Ovarian Cancer.
    Cancers (Basel). 12(3): 707.
  22. Komulainen, E. et al. (2021) Parp1 hyperactivity couples DNA breaks to aberrant neuronal calcium signalling and lethal seizures.
    EMBO Rep. 22 (5): e51851.
  23. Rosso, I. et al. (2023) Alternative lengthening of telomeres (ALT) cells viability is dependent on C-rich telomeric RNAs.
    Nat Commun. 14 (1): 7086.

Further Reading

  1. 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.
  2. Rosado, M. et al. (2013) Beyond dna repair,the immunological role of parp-1 and its siblings.
    Immunology. 139: 428-37.
  3. Andreone, T. et al. (2012) Cytokine-mediatedβ-cell damage in PARP-1-deficient islets.
    Am J Physiol Endocrinol Metab. 303: E172-9.
  4. 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.

Immunohistology - Paraffin

Western Blotting

RRID
AB_2236751
UniProt
P09874
Entrez Gene
PARP1
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
GO:0042802 identical protein binding
GO:0032869 cellular response to insulin stimulus
GO:0045449 regulation of transcription
GO:0047485 protein N-terminus binding

MCA1522G

156107 1806

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