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

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Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 thumbnail image 1 Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 thumbnail image 2 Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 thumbnail image 3 Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 thumbnail image 4 Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 thumbnail image 5 Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 thumbnail image 6 Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 thumbnail image 7 Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 thumbnail image 8
Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 gallery image 1
HeLa Nuclear Extract probed with Mouse anti Poly (ADP-Ribose) Polymerase (MCA1522G)
Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 gallery image 2
Western blot analysis of HEK293 whole cell lysate probed with Mouse anti Human poly(ADP-ribose) polymerase-1 antibody (MCA1522G) followed by HRP conjugated Goat anti Mouse IgG, visualized using chemiluminescence
Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 gallery image 3
Published customer image:
Mouse anti poly (ADP-ribose) polymerase 1 antibody, clone A6.4.12 used to immunolocalize PARP-1 expression in normal and Alzheimer's diseased brain by immunohistochemistry on formalin fixed paraffin embedded tissue sections.
Image caption:
Nucleolar PARP-1 immunoreactivity in AD ranged from absent to dispersed and less intense compared to that of controls. ((a) and (b)) Representative immunostaining with diaminobenzidine (DAB) of human hippocampal pyramidal neurons in CA1 region. (a) Prominent nucleolar staining of PARP-1 (arrows) was seen in most of pyramidal neurons of a control case. (b) The nucleolar staining of PARP-1 ranged from absent (arrowheads) to a more dispersed pattern with less intensity of label (arrows) in pyramidal neurons of an AD case.

From: Jianying Zeng, Jenny Libien, Fatima Shaik, Jason Wolk, and A. Iván Hernández,
“Nucleolar PARP-1 Expression Is Decreased in Alzheimer's Disease: Consequences for Epigenetic Regulation of rDNA and Cognition,”
Neural Plasticity, vol. 2016, Article ID 8987928.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 gallery image 4
Published customer image:
Mouse anti poly (ADP-ribose) polymerase 1 antibody, clone A6.4.12 used to immunolocalize PARP-1 expression in normal and Alzheimer's diseased brain by immunofluorescence on formalin fixed paraffin embedded tissue sections.
Image caption:
PARP-1 nucleolar immunoreactivity is altered in hippocampal pyramidal cells in AD brains. Representative confocal microscopy of PARP-1 immunostaining (red) with DAPI nuclear counterstaining (blue) of CA4 hippocampal pyramidal neurons. In controls brains (a–c) a high percentage of pyramidal cell nucleoli have intense and well- delineated PARP-1 staining (arrowheads). In contrast, in AD brains (d–f), the percentage of intensely stained and well-delineated nucleoli is less than in the controls and there is a more dispersed pattern with weak label intensity ((d) and (f), arrow). ((g) and (h)) The percentage of CA1 (g) and CA4 (h) hippocampal pyramidal neurons with PARP-1 positive nucleoli staining was less in AD cases compared to controls. (Control, and for CA1 and CA4, resp.; AD, for both CA1 and CA4; .) Scale bar = 25 μM.

From: Jianying Zeng, Jenny Libien, Fatima Shaik, Jason Wolk, and A. Iván Hernández,
“Nucleolar PARP-1 Expression Is Decreased in Alzheimer's Disease: Consequences for Epigenetic Regulation of rDNA and Cognition,”
Neural Plasticity, vol. 2016, Article ID 8987928.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 gallery image 5
Published customer image:
Mouse anti poly (ADP-ribose) polymerase 1 antibody, clone A6.4.12 used to immunolocalize PARP-1 expression in normal and Alzheimer's diseased brain by immunohistochemistry on formalin fixed paraffin embedded tissue sections.
Image caption:
Nucleolar proteins in hippocampal pyramidal cells are altered in AD. ((a)–(h)) Representative figures show colocalization ((d) and (h), yellow) of fibrillarin ((b) and (f), green) and PARP-1 ((c) and (g), red) in the nucleoli of pyramidal neurons. Control cases exhibit high intensity staining (a–d) compared to AD (e–h) (arrowheads). In AD compared to controls, there is a lower percentage of nucleoli that are both PARP-1(+) and fibrillarin(+) ((f)-(g), arrowhead) in CA1 (see Table 2) and CA4 (see Table 3) pyramidal cells and a higher percentage of nucleoli PARP-1(−)/fibrillarin(+) ((f) and (g), arrow) in CA1 (see Table 2) and CA4 (see Table 3), suggesting that different nucleolar proteins are affected in different ways in AD. Scale bar = 20 μm.

From: Jianying Zeng, Jenny Libien, Fatima Shaik, Jason Wolk, and A. Iván Hernández,
“Nucleolar PARP-1 Expression Is Decreased in Alzheimer's Disease: Consequences for Epigenetic Regulation of rDNA and Cognition,”
Neural Plasticity, vol. 2016, Article ID 8987928.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 gallery image 6
Published customer image:
Mouse anti poly(ADP-ribose) polymerase-1 antibody, clone A6.4.12 (MCA1522G) used for the evaluation of PARP-1 expression in murine neural stem/progenitor cell populations by western blotting.
Image caption:
Higher amounts of p53 protein and phosphorylated p53 in NSPCs after PARP inhibition. a Cleaved fragments of caspase-3 (p17) and caspase-8 (p43/p41/p18) were clearly detectable by western blotting with specific antibodies. The cleaved fragment of pro-caspase-9 (p37) was also detectable, although the band density of this fragment was low. b Phase-contrast images were shown on the top. Higher amounts of p53 protein and phosphorylated p53 in NSPCs after PARP inhibition were also revealed by immunocytochemistry. Representative images from 4 separate experiments are shown. c Western blot analysis demonstrated that PARP-1 was abundant and activated in NSPCs in contrast to MEFs. Amounts of p53 protein and phosphorylated p53 at Ser 18 were remarkably increased by PJ34. Scale bars in (b), 20μm.

From: Okuda A, Kurokawa S, Takehashi M, Maeda A, Fukuda K, Kubo Y, Nogusa H, Takatani-Nakase T, Okuda S, Ueda K, Tanaka S.
Poly(ADP-ribose) polymerase inhibitors activate the p53 signaling pathway in neural stem/progenitor cells.
BMC Neurosci. 2017 Jan 17;18(1):14.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 gallery image 7
Published customer image:
Mouse anti Human PARP-1 antibody, clone A6.4.12 (MCA1522G) used for the evaluation of PAR-1 expression on wild type and knockout hTERT immortalized retinal pigment epithelial cels by westrn blotting and immunofluorescence.
Image caption:
Development of PARP1-/-, PARP2-/-, PARP3-/- and XRCC1-/- RPE-1 cells and XRCC1 high-content imaging. Wild type (WT), PARP1-/-, PARP2-/-, PARP3-/- and XRCC1-/- RPE-1 clonal cell lines were analysed for loss of the targeted protein by (A) Western blotting and (B) immunofluorescence. Note that the PARP3 antibody available to us was not suitable for immunofluorescence.

From: Hanzlikova H, Gittens W, Krejcikova K, Zeng Z, Caldecott KW.
Overlapping rolesfor PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin.
Nucleic Acids Res. 2017 Mar 17;45(5):2546-2557.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.
Anti Poly(ADP-Ribose) Polymerase-1 Antibody, clone A6.4.12 gallery image 8
Published customer image:
Mouse anti Human PARP-1 antibody, clone A6.4.12 (MCA1522G) used for the evaluation of PAR-1 expression on wild type and knockout hTERT immortalized retinal pigment epithelial cells by western blotting.
Image caption:
Levels of H2O2-induced ADP-ribosylation and XRCC1 recruitment into chromatin in PARP-deleted RPE-1 cells. (A) Levels of the indicated proteins (left) and ADP-ribosylated proteins (right) were compared in cell lysates from the indicated WT or mutant RPE-1 cells harvested before and after treatment with 400 μM H2O2 for 7 min by Western blotting using appropriate antibodies and anti-pan-ADP-ribose binding reagent. (B) Levels of ADP-ribosylation and chromatin-bound XRCC1 were analysed by indirect immunofluorescence in cells treated or not with H2O2 (as above) by fixation and staining with anti-pan-ADP-ribose binding reagent (top panels) or by detergent pre-extraction prior to fixation and staining with anti-XRCC1 antibody (bottom panels). Representative ScanR images are shown.

From: Hanzlikova H, Gittens W, Krejcikova K, Zeng Z, Caldecott KW.
Overlapping rolesfor PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin.
Nucleic Acids Res. 2017 Mar 17;45(5):2546-2557.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.

Mouse anti Poly(ADP-Ribose) Polymerase-1

Product Type
Monoclonal Antibody
Clone
A6.4.12
Isotype
IgG1
Product Code Applications Pack Size List Price Quantity
MCA1522G
Datasheet
C E IF IP P* WB
MSDS
0.1 mg 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).

Product Details

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
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.

Storage Information

Storage
Store at +4oC or at -20oC if preferred.

This product should be stored undiluted.

Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
Guarantee
12 months from date of despatch

More Information

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
Regulatory
For research purposes only

Applications of Poly(ADP-Ribose) Polymerase-1 antibody

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 antibody 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 antibody for use in their own system using appropriate negative/positive controls.

Copyright © 2020 Bio-Rad Antibodies (formerly AbD Serotec)

Secondary Antibodies Available

Description Product Code Applications Pack Size List Price Quantity
Goat anti Mouse IgG (H/L):Alk. Phos. (Multi Species Adsorbed) STAR117A E WB 0.5 mg loader
Goat anti Mouse IgG (H/L):DyLight®488 (Multi Species Adsorbed) STAR117D488GA F IF 0.1 mg loader
Goat anti Mouse IgG (H/L):DyLight®680 (Multi Species Adsorbed) STAR117D680GA F WB 0.1 mg loader
Goat anti Mouse IgG (H/L):DyLight®800 (Multi Species Adsorbed) STAR117D800GA F IF WB 0.1 mg loader
Goat anti Mouse IgG (H/L):FITC (Multi Species Adsorbed) STAR117F F 0.5 mg loader
Goat anti Mouse IgG (H/L):HRP (Multi Species Adsorbed) STAR117P E WB 0.5 mg loader
Goat anti Mouse IgG (Fc):FITC STAR120F C F 1 mg loader
Goat anti Mouse IgG (Fc):HRP STAR120P E WB 1 mg loader
Rabbit F(ab')2 anti Mouse IgG:RPE STAR12A F 1 ml loader
Rabbit F(ab')2 anti Mouse IgG:HRP (Human Adsorbed) STAR13B C E P RE WB 1 mg loader
Goat anti Mouse IgG:FITC (Rat Adsorbed) STAR70 F 0.5 mg loader
Goat anti Mouse IgG:RPE (Rat Adsorbed) STAR76 F 1 ml loader
Goat anti Mouse IgG:HRP (Rat Adsorbed) STAR77 C E P 0.5 mg loader
Goat anti Mouse IgG/A/M:Alk. Phos. STAR87A C E WB 1 mg loader
Goat anti Mouse IgG/A/M:HRP (Human Adsorbed) STAR87P E 1 mg loader
Rabbit F(ab')2 anti Mouse IgG:Dylight®800 STAR8D800GA F IF WB 0.1 mg loader
Rabbit F(ab')2 anti Mouse IgG:FITC STAR9B F 1 mg loader

Application Based External Images

Immunohistology - Paraffin

Western Blotting

Product Specific References

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. 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.
  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. et al. (2012) PARP and adjuvant cisplatin-based chemotherapy in non-small-cell lung cancer.
    US patent: 20120277110
  12. Geistrikh, I. et al. (2011) Ca2+-induced PARP-1 activation and ANF expression are coupled events in cardiomyocytes.
    Biochem J. 438: 337-47.
  13. Mirzaa, G.M. et al. (2014) Mutations in CENPE define a novel kinetochore-centromeric mechanism for microcephalic primordial dwarfism.
    Hum Genet. 133: 1023-39.
  14. 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.
  15. Inbar, D. et al. (2012) Erythropoietin-driven signalling and cell migration mediated by polyADP-ribosylation.
    Br J Cancer. 107: 1317-26.
  16. Buchsbaum, S. et al. (2012) FAT10 is a proteasomal degradation signal that is itself regulated by ubiquitination.
    Mol Biol Cell. 23: 225-32.
  17. 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.
  18. 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.
  19. 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.

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.

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