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AB137653

Anti-PARP1 antibody

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(17 Publications )

Rabbit Polyclonal PARP1 antibody. Suitable for ChIP, WB, ICC/IF, IHC-P and reacts with Human, Rat samples. Cited in 17 publications. Immunogen corresponding to Recombinant Fragment Protein within Human PARP1 aa 150-450.

View Alternative Names

ADPRT, PPOL, PARP1, Poly [ADP-ribose] polymerase 1, PARP-1, ADP-ribosyltransferase diphtheria toxin-like 1, DNA ADP-ribosyltransferase PARP1, NAD(+) ADP-ribosyltransferase 1, Poly[ADP-ribose] synthase 1, Protein poly-ADP-ribosyltransferase PARP1, ARTD1, ADPRT 1

6 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PARP1 antibody (AB137653)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-PARP1 antibody (AB137653)

Paraffin-embedded human oral carcinoma tissue stained for PARP1 protein at nucleus in human oral carcinoma with ab137653 at a 1/500 dilution in immunohistochemical analysis.

Antigen Retrieval : Citrate buffer, pH 6.0, 15 min

Immunocytochemistry/ Immunofluorescence - Anti-PARP1 antibody (AB137653)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-PARP1 antibody (AB137653)

Immunofluorescence analysis of 4% paraformaldehyde fixed HeLa cells labelling PARP1 protein at nucleus using ab137653 at a 1/500 dilution at RT for 15 min (Green). Phalloidin, a cytoskeleton marker was used to counterstain Phalloidin diluted at 1/100 dilution (Red).
Scale bar = 10 µm

ChIP - Anti-PARP1 antibody (AB137653)
  • ChIP

Supplier Data

ChIP - Anti-PARP1 antibody (AB137653)

Cross-linked ChIP was performed with Raji chromatin extract and 5 μg of either control rabbit IgG or anti-PARP11 antibody. The precipitated DNA was detected by PCR with primer set targeting to S100A9 promoter.ChIP experiment and primer designs are based on BMC Mol Biol. 2006 Dec 22;7 : 48.

Western blot - Anti-PARP1 antibody (AB137653)
  • WB

Unknown

Western blot - Anti-PARP1 antibody (AB137653)

7.5% SDS PAGE

All lanes:

Western blot - Anti-PARP1 antibody (ab137653) at 1/1000 dilution

Lane 1:

HCT116 whole cell lysate/extract (untreated) at 30 µg

Lane 2:

HCT116 whole cell lysate/extract (30 µM cisplatin treatment for 24hr) at 30 µg

Predicted band size: 113 kDa

false

Western blot - Anti-PARP1 antibody (AB137653)
  • WB

Supplier Data

Western blot - Anti-PARP1 antibody (AB137653)

Samples were separated by 12% SDS-PAGE.

All lanes:

Western blot - Anti-PARP1 antibody (ab137653) at 1/50000 dilution

Lane 1:

Non-transfected 293T cells at 30 µg

Lane 2:

Transfected DDDK-tagged PARP1 293T cells at 30 µg

Lane 3:

Transfected DDDK-tagged PARP2 293T cells at 30 µg

Lane 4:

Transfected DDDK-tagged PARP3 293T cells at 30 µg

Secondary

All lanes:

HRP-conjugated anti-rabbit IgG antibody

Predicted band size: 113 kDa

false

Western blot - Anti-PARP1 antibody (AB137653)
  • WB

Supplier Data

Western blot - Anti-PARP1 antibody (AB137653)

Samples were separated by 7.5% SDS-PAGE.

All lanes:

Western blot - Anti-PARP1 antibody (ab137653) at 1/2000 dilution

Lane 1:

Untreated HeLa whole cell extracts at 30 µg

Lane 2:

Treated HeLa whole cell extracts at 30 µg

Secondary

All lanes:

HRP-conjugated anti-rabbit IgG antibody

Predicted band size: 113 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human, Rat

Applications

WB, ChIP, IHC-P, ICC/IF

applications

Immunogen

Recombinant Fragment Protein within Human PARP1 aa 150-450. The exact immunogen used to generate this antibody is proprietary information.

P09874

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ChIP" : {"fullname" : "ChIP", "shortname":"ChIP"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "ChIP-species-checked": "testedAndGuaranteed", "ChIP-species-dilution-info": "", "ChIP-species-notes": "<p></p>", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/3000", "WB-species-notes": "<p></p>", "ICCIF-species-checked": "testedAndGuaranteed", "ICCIF-species-dilution-info": "1/100 - 1/1000", "ICCIF-species-notes": "<p></p>", "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "1/100 - 1/1000", "IHCP-species-notes": "<p></p>" }, "Rat": { "ChIP-species-checked": "guaranteed", "ChIP-species-dilution-info": "", "ChIP-species-notes": "", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/3000", "WB-species-notes": "<p></p>", "ICCIF-species-checked": "guaranteed", "ICCIF-species-dilution-info": "", "ICCIF-species-notes": "", "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.025% Proclin 300 Constituents: PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PARP1 also known as poly(ADP-ribose) polymerase 1 is an enzyme that plays an important role in DNA repair processes. It detects DNA single-strand breaks and uses NAD+ as a substrate to add ADP-ribose polymers to itself and other proteins. This post-translational modification signals DNA repair machinery to the site of damage. PARP1 has a molecular weight of approximately 116 kDa. It is widely expressed in the nucleus of eukaryotic cells. PARP1 is often studied by western blotting techniques to analyze its expression and activation levels.
Biological function summary

Poly(ADP-ribose) polymerase 1 functions to maintain genomic stability by acting within the base excision repair complex. This complex is important for the detection and repair of DNA damage preventing the accumulation of mutations. By acting at sites of DNA stress PARP1 facilitates the binding of DNA repair proteins stabilizing the DNA structure during the repair process. This role is significant for cells that undergo frequent DNA replication or are exposed to high levels of genotoxic stress.

Pathways

The PARP1 protein is integral to the DNA damage response and repair pathway. It interacts with other proteins such as XRCC1 to coordinate repair activities at damaged DNA sites. Another important pathway involving PARP1 is the apoptosis pathway where excessive activation of PARP1 can lead to cell death due to depletion of cellular NAD+ and ATP. This indicates its dual role in both promoting cell survival through DNA repair and contributing to cell death when damage is irreparable.

Poly(ADP-ribose) polymerase 1 is strongly linked to cancer and neurodegenerative diseases. Its activity is heightened in many cancer types where cancer cells exploit PARP1 for survival by repairing DNA damage that would otherwise be lethal. Inhibitors of PARP1 are being developed as cancer therapies to target these survival mechanisms. Moreover overactivation of PARP1 in neurodegenerative disorders like Alzheimer's disease can lead to excessive energy consumption promoting neuronal cell damage. In these contexts PARP1 connects with proteins like BRCA1 in cancer or AIF in neurodegeneration illustrating its role in disease mechanisms.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed : 17177976, PubMed : 18055453, PubMed : 18172500, PubMed : 19344625, PubMed : 19661379, PubMed : 20388712, PubMed : 21680843, PubMed : 22582261, PubMed : 23230272, PubMed : 25043379, PubMed : 26344098, PubMed : 26626479, PubMed : 26626480, PubMed : 30104678, PubMed : 31796734, PubMed : 32028527, PubMed : 32241924, PubMed : 32358582, PubMed : 33186521, PubMed : 34465625, PubMed : 34737271). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins : the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed : 19764761, PubMed : 25043379, PubMed : 28190768, PubMed : 29954836, PubMed : 35393539, PubMed : 7852410, PubMed : 9315851). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed : 33186521, PubMed : 34874266). Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 (PubMed : 28190768, PubMed : 29954836, PubMed : 32028527, PubMed : 33186521, PubMed : 33589610, PubMed : 34625544, PubMed : 34874266). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site (PubMed : 28190768, PubMed : 29954836, PubMed : 32028527, PubMed : 33186521, PubMed : 33589610, PubMed : 34625544, PubMed : 34874266). Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed : 29954836, PubMed : 30257210). Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks : recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed : 17177976, PubMed : 18172500, PubMed : 19344625, PubMed : 19661379, PubMed : 23230272, PubMed : 27067600, PubMed : 34465625, PubMed : 34874266). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains (PubMed : 33683197, PubMed : 34732825, PubMed : 34795260). In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair : together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation (PubMed : 26344098, PubMed : 30356214). Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR, RPA1 and NFAT5 (PubMed : 17396150, PubMed : 19764761, PubMed : 24906880, PubMed : 34049076). In addition to proteins, also able to ADP-ribosylate DNA : catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (PubMed : 27471034). Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed : 23230272). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed : 23230272). PARP1-mediated DNA repair in neurons plays a role in sleep : senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (PubMed : 15607977, PubMed : 17177976, PubMed : 19344625, PubMed : 27256882, PubMed : 32315358, PubMed : 32844745, PubMed : 35124853, PubMed : 35393539, PubMed : 35460603). Acts as a repressor of transcription : binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II (PubMed : 15607977, PubMed : 22464733). Acts both as a positive and negative regulator of transcription elongation, depending on the context (PubMed : 27256882, PubMed : 35393539). Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing (PubMed : 27256882). Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 (PubMed : 35393539). Involved in replication fork progression following interaction with CARM1 : mediates poly-ADP-ribosylation at replication forks, slowing fork progression (PubMed : 33412112). Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity). Also acts as a negative regulator of the cGAS-STING pathway (PubMed : 32315358, PubMed : 32844745, PubMed : 35460603). Acts by mediating poly-ADP-ribosylation of CGAS : PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS (PubMed : 35460603). Acts as a negative regulator of adipogenesis : catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed : 27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed : 27257257).. Poly [ADP-ribose] polymerase 1, processed C-terminus. Promotes AIFM1-mediated apoptosis (PubMed : 33168626). This form, which translocates into the cytoplasm following cleavage by caspase-3 (CASP3) and caspase-7 (CASP7) in response to apoptosis, is auto-poly-ADP-ribosylated and serves as a poly-ADP-ribose carrier to induce AIFM1-mediated apoptosis (PubMed : 33168626).. Poly [ADP-ribose] polymerase 1, processed N-terminus. This cleavage form irreversibly binds to DNA breaks and interferes with DNA repair, promoting DNA damage-induced apoptosis.
See full target information PARP1
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Publications (17)

Recent publications for all applications. Explore the full list and refine your search

Apoptosis : an international journal on programmed cell death 29:2197-2213 PubMed39222276

2024

BH3-mimetics or DNA-damaging agents in combination with RG7388 overcome p53 mutation-induced resistance to MDM2 inhibition.

Applications

Unspecified application

Species

Unspecified reactive species

N V Pervushin,D K Nilov,S V Pushkarev,V O Shipunova,A S Badlaeva,M A Yapryntseva,D V Kopytova,B Zhivotovsky,G S Kopeina

Nutrients 16: PubMed39125387

2024

Health-Promoting Effects, Phytochemical Constituents and Molecular Genetic Profile of the Purple Carrot 'Purple Sun' ( L.).

Applications

Unspecified application

Species

Unspecified reactive species

Viviana Maresca,Lucia Capasso,Daniela Rigano,Mariano Stornaiuolo,Carmina Sirignano,Sonia Piacente,Antonietta Cerulli,Nadia Marallo,Adriana Basile,Angela Nebbioso,Deborah Giordano,Angelo Facchiano,Luigi De Masi,Paola Bontempo

Haematologica 108:3333-3346 PubMed37381763

2023

Long non-coding RNA mitophagy and ALK-negative anaplastic lymphoma-associated transcript: a novel regulator of mitophagy in T-cell lymphoma.

Applications

Unspecified application

Species

Unspecified reactive species

Valentina Mularoni,Benedetta Donati,Annalisa Tameni,Veronica Manicardi,Francesca Reggiani,Elisabetta Sauta,Magda Zanelli,Marco Tigano,Emanuele Vitale,Federica Torricelli,Stefano Ascani,Giovanni Martino,Giorgio Inghirami,Francesca Sanguedolce,Alessia Ruffini,Alberto Bavieri,Stefano Luminari,Marco Pizzi,Angelo Paolo Dei Tos,Cinzia Fesce,Antonino Neri,Alessia Ciarrocchi,Valentina Fragliasso

Cell death discovery 8:417 PubMed36241623

2022

Drug toxicity assessment: cell proliferation versus cell death.

Applications

Unspecified application

Species

Unspecified reactive species

Elena V Sazonova,Mikhail S Chesnokov,Boris Zhivotovsky,Gelina S Kopeina

Oncology letters 24:392 PubMed36276487

2022

Effect of the PARP inhibitor veliparib on germ cell tumor cell lines.

Applications

Unspecified application

Species

Unspecified reactive species

Silvia Schmidtova,Natalia Udvorkova,Zuzana Cierna,Samuel Horak,Katarina Kalavska,Michal Chovanec,Lucia Rojikova,Miriam Vulevova,Lucia Kucerova,Michal Mego

Frontiers in pharmacology 13:962763 PubMed36016563

2022

Raman and fluorescence micro-spectroscopy applied for the monitoring of sunitinib-loaded porous silicon nanocontainers in cardiac cells.

Applications

Unspecified application

Species

Unspecified reactive species

E Tolstik,M B Gongalsky,J Dierks,T Brand,M Pernecker,N V Pervushin,D E Maksutova,K A Gonchar,J V Samsonova,G Kopeina,V Sivakov,L A Osminkina,K Lorenz

International journal of molecular sciences 23: PubMed35409093

2022

Necroptosis as a Novel Facet of Mitotic Catastrophe.

Applications

Unspecified application

Species

Unspecified reactive species

Aleksandra Yu Egorshina,Alexey V Zamaraev,Vitaliy O Kaminskyy,Tatiana V Radygina,Boris Zhivotovsky,Gelina S Kopeina

Nanomaterials (Basel, Switzerland) 11: PubMed34578485

2021

Optical Monitoring of the Biodegradation of Porous and Solid Silicon Nanoparticles.

Applications

Unspecified application

Species

Unspecified reactive species

Maxim B Gongalsky,Nikolay V Pervushin,Daria E Maksutova,Uliana A Tsurikova,Pavel P Putintsev,Oleg D Gyuppenen,Yana V Evstratova,Olga A Shalygina,Gelina S Kopeina,Andrey A Kudryavtsev,Boris Zhivotovsky,Liubov A Osminkina

Frontiers in cell and developmental biology 9:621134 PubMed34095104

2021

PARP1 Regulates the Biogenesis and Activity of Telomerase Complex Through Modification of H/ACA-Proteins.

Applications

Unspecified application

Species

Unspecified reactive species

Nikita V Savelyev,Nikita M Shepelev,Olga I Lavrik,Maria P Rubtsova,Olga A Dontsova

Frontiers in cell and developmental biology 8:543066 PubMed33072738

2020

Upregulation of Mcl-1S Causes Cell-Cycle Perturbations and DNA Damage Accumulation.

Applications

Unspecified application

Species

Unspecified reactive species

Alena Y Streletskaia,Viacheslav V Senichkin,Tatiana A Prikazchikova,Timofei S Zatsepin,Boris Zhivotovsky,Gelina S Kopeina
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