PARP1 Antibody - #DF7198

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Product: PARP1 Antibody
Catalog: DF7198
Description: Rabbit polyclonal antibody to PARP1
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 89kDa(cleaved), 113kDa(precursor); 113kD(Calculated).
Uniprot: P09874
RRID: AB_2839150

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MS Report
HPLC Report
MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Rabbit
Application:
WB 1:500-1:1000, IHC 1:50-1:100, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Zebrafish(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
PARP1 Antibody detects endogenous levels of total PARP1.
RRID:
AB_2839150
Cite Format: Affinity Biosciences Cat# DF7198, RRID:AB_2839150.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

ADP-ribosyltransferase diphtheria toxin-like 1; ADPRT 1; ADPRT; ADPRT1; APOPAIN; ARTD1; NAD(+) ADP-ribosyltransferase 1; PARP; PARP-1; PARP1; PARP1_HUMAN; Poly [ADP-ribose] polymerase 1; Poly ADP ribose polymerase 1; Poly[ADP-ribose] synthase 1; PPOL; SCA1;

Immunogens

Immunogen:
Uniprot:

P09874(PARP1_HUMAN) >>Visit HPA database.

Gene(ID):
PARP1(142)
Description:
PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).
Sequence:
MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Xenopus
100
Zebrafish
100
Chicken
100
Rabbit
100
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P09874 As Substrate

Site PTM Type Enzyme
A2 Acetylation
S5 Phosphorylation
K7 Ubiquitination
K15 Ubiquitination
S16 Phosphorylation
C24 S-Nitrosylation
S25 Phosphorylation
S27 Phosphorylation
S32 Phosphorylation
S41 Phosphorylation
R65 Methylation
S75 Phosphorylation
R78 Methylation
K84 Acetylation
K84 Ubiquitination
K87 Ubiquitination
T88 Phosphorylation
K97 Acetylation
K97 Sumoylation
K97 Ubiquitination
K105 Acetylation
K105 Sumoylation
K108 Acetylation
K108 Ubiquitination
Y117 Phosphorylation
K119 Ubiquitination
K131 Acetylation
K131 Ubiquitination
K148 Acetylation
K148 Sumoylation
K148 Ubiquitination
R156 Methylation
K165 Ubiquitination
S177 Phosphorylation P54646 (PRKAA2)
S179 Phosphorylation
K182 Ubiquitination
S185 Phosphorylation
T189 Phosphorylation
K192 Sumoylation
K192 Ubiquitination
K197 Ubiquitination
K203 Sumoylation
S204 Phosphorylation
K209 Ubiquitination
K221 Ubiquitination
S224 Phosphorylation
K239 Ubiquitination
K249 Acetylation
K249 Sumoylation
K249 Ubiquitination
K253 Acetylation
K254 Acetylation
K254 Ubiquitination
S257 Phosphorylation
K262 Acetylation
K262 Sumoylation
K262 Ubiquitination
K269 Ubiquitination
S274 Phosphorylation
S277 Phosphorylation
R282 Methylation
K320 Ubiquitination
K331 Ubiquitination
K337 Sumoylation
K337 Ubiquitination
S343 Phosphorylation
S362 Phosphorylation
S364 Phosphorylation
T368 Phosphorylation
S372 Phosphorylation P28482 (MAPK1)
T373 Phosphorylation P28482 (MAPK1)
S375 Phosphorylation
S391 Phosphorylation
K394 Ubiquitination
K400 Acetylation
K400 Ubiquitination
K409 Sumoylation
K414 Ubiquitination
K418 Acetylation
K418 Ubiquitination
T420 Phosphorylation
K425 Ubiquitination
K433 Acetylation
K433 Sumoylation
K434 Ubiquitination
K447 Ubiquitination
S455 Phosphorylation
S465 Phosphorylation
K467 Sumoylation
S479 Phosphorylation
K486 Sumoylation
K486 Ubiquitination
K498 Acetylation
S499 Phosphorylation
S504 Phosphorylation
K505 Acetylation
K508 Acetylation
K508 Methylation
K512 Sumoylation
K518 Acetylation
K518 Sumoylation
S519 Phosphorylation
K521 Acetylation
K524 Acetylation
K528 Sumoylation
K528 Ubiquitination
S537 Phosphorylation
S542 Phosphorylation
K548 Acetylation
K548 Ubiquitination
K551 Ubiquitination
K564 Ubiquitination
K571 Ubiquitination
K579 Acetylation
K579 Ubiquitination
R582 Methylation
K600 Acetylation
K600 Sumoylation
K600 Ubiquitination
S606 Phosphorylation
K607 Ubiquitination
K621 Acetylation
K621 Ubiquitination
K629 Acetylation
K629 Ubiquitination
K633 Acetylation
K633 Ubiquitination
K637 Sumoylation
K637 Ubiquitination
Y645 Phosphorylation
K653 Ubiquitination
K654 Sumoylation
K654 Ubiquitination
T661 Phosphorylation
K662 Ubiquitination
K664 Ubiquitination
K667 Ubiquitination
K674 Methylation
S681 Phosphorylation
K683 Acetylation
Y689 Phosphorylation
K695 Ubiquitination
K700 Ubiquitination
S702 Phosphorylation
S733 Phosphorylation
Y737 Phosphorylation
T738 Phosphorylation
K748 Sumoylation
K748 Ubiquitination
Y775 Phosphorylation
R779 Methylation
S782 Phosphorylation
S785 Phosphorylation
S786 Phosphorylation
K787 Ubiquitination
Y794 Phosphorylation
K796 Sumoylation
K796 Ubiquitination
K798 Ubiquitination
R806 Methylation
S808 Phosphorylation
R815 Methylation
K819 Ubiquitination
T824 Phosphorylation
K838 Ubiquitination
K852 Acetylation
K852 Ubiquitination
S864 Phosphorylation
S874 Phosphorylation
R878 Methylation
Y896 Phosphorylation
Y907 Phosphorylation P08581 (MET)
K940 Ubiquitination
K949 Ubiquitination
K1010 Methylation
K1010 Ubiquitination

Research Backgrounds

Function:

Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of glutamate and aspartate 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. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity. Probably also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. Catalyzes the poly-ADP-ribosylation of histones in a HPF1-dependent manner. Involved in the base excision repair (BER) pathway by catalyzing the poly-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. 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. 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. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.

PTMs:

Phosphorylated by PRKDC and TXK.

Poly-ADP-ribosylated on glutamate and aspartate residues by autocatalysis. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites. ADP-ribosylated on serine by autocatalysis; serine ADP-ribosylation takes place following interaction with HPF1.

S-nitrosylated, leading to inhibit transcription regulation activity.

Subcellular Location:

Nucleus. Nucleus>Nucleolus. Chromosome.
Note: Localizes to sites of DNA damage.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Homo- and heterodimer with PARP2. Interacts with APTX. Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, PARP2, POLB and LRIG3 (By similarity). Interacts with SRY. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 (By similarity). Interacts with TIAM2 (By similarity). Interacts with PARP3; leading to activate PARP1 in absence of DNA. Interacts (when poly-ADP-ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression. Interacts with EEF1A1 and TXK. Interacts with RNF4. Interacts with RNF146. Interacts with ZNF423. Interacts with APLF. Interacts with SNAI1 (via zinc fingers); the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (when poly-ADP-ribosylated) with PARP9. Interacts with NR4A3; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1 (By similarity). Interacts (via catalytic domain) with PUM3; the interaction inhibits the poly-ADP-ribosylation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress. Interacts (via the PARP catalytic domain) with HPF1. Interacts with ZNF365. Interacts with RRP1B. Interacts with TIMELESS; the interaction is direct. Interacts with CGAS; leading to impede the formation of the PARP1-TIMELESS complex.

Research Fields

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Cellular Processes > Cell growth and death > Necroptosis.   (View pathway)

· Environmental Information Processing > Signal transduction > NF-kappa B signaling pathway.   (View pathway)

· Genetic Information Processing > Replication and repair > Base excision repair.

References

1). Upregulation of BCL-2 by acridone derivative through gene promoter i-motif for alleviating liver damage of NAFLD/NASH. NUCLEIC ACIDS RESEARCH, 2020 (PubMed: 32710621) [IF=14.9]

Application: WB    Species: mouse    Sample: liver

Figure 7. Effect of A22 on ameliorating apoptosis, ER stress, inflammation, metabolic syndrome, and fibrogenesis in HF diet-fed mice. (A) Effect of A22 on BCL-2 gene transcription. (B) Effect of A22 on BAX gene transcription. (C) Effect of A22 on expressions of apoptosis-related proteins in liver. The extracted proteins from the liver were immunoblotted with specific antibodies, and quantified based on the loading control of ACTIN. (D) Effect of A22 on ER stress. The UPR proteins (IRE-1, PERK, elF-2 and CHOP) were analyzed by using western Blot. (E) Effect of A22 on expressions of inflammatory factors. (F) Effect of A22 on expressions of fibrogenic proteins.
2). Cooperative STAT3-NFkB signaling modulates mitochondrial dysfunction and metabolic profiling in hepatocellular carcinoma. Metabolism: clinical and experimental, 2024 (PubMed: 38184165) [IF=9.8]
3). Danhong injection alleviates cerebral ischemia/reperfusion injury by improving intracellular energy metabolism coupling in the ischemic penumbra. Biomedicine & Pharmacotherapy, 2021 (PubMed: 34058441) [IF=7.5]

Application: WB    Species: rat    Sample:

Fig. 4.| Effect of DHI on the activity of PARP1/AIF signaling pathway and the content of molecules associated with cytoplasmic glycolysis. A-E: Representative images of WB analysis and the semi-quantification of PARP1, PAR, AIF, and HSP70. Data are expressed as mean ± SD (n = 3).

Application: IHC    Species: rat    Sample: brain

Fig. 5.| Effect of DHI on the content of molecules associated with cytoplasmic glycolysis. A-F: Immunostaining photomicrographs of PARP1, AIF, HSP70 and quantitative analysis of the IOD.
4). Perilla frutescens L. alleviates trimethylamine N-oxide–induced apoptosis in the renal tubule by regulating ASK1-JNK phosphorylation. Phytotherapy Research, 2023 (PubMed: 36420586) [IF=7.2]
5). Exploring the Critical Components and Therapeutic Mechanisms of Perilla frutescens L. in the Treatment of Chronic Kidney Disease via Network Pharmacology. Frontiers in Pharmacology, 2021 (PubMed: 34899287) [IF=5.6]

Application: WB    Species: Rat    Sample: NRK-52E cells

FIGURE 8 Luteolin reduces ADR-induced apoptosis. (A) Effects of luteolin in ADR-induced apoptosis by TUNEL and DAPI staining assay. NRK-52E cells were incubated with ADR for 24 h in the presence and absence of luteolin. Apoptotic cells were detected by TUNEL and DAPI staining. Fluorescence staining was observed by fluorescence microscope (magnification ×200) and the analysis result on the right was expressed as the percentages of dead cells compared with the Ctrl (mean ± SD, n = 3; *p
6). Oligo-Porphyran Ameliorates Neurobehavioral Deficits in Parkinsonian Mice by Regulating the PI3K/Akt/Bcl-2 Pathway. Marine Drugs, 2018 (PubMed: 29509717) [IF=5.4]

Application: WB    Species: mouse    Sample:

Figure 5. | Effects on apoptosis-related protein expression, poly ADP ribose polymerase (PARP), and caspase-3 activity in vivo. After pretreated with MPTP for seven days, the C57BL/6 mice were administrated with MA or different concentrations of OP for the followed 7 days. (A): Original bands of cytochrome c (CytC), cleaved caspased-3, B-cell lymphoma 2 (Bcl-2), BCL2 associated X (Bax), PARP, and β-actin.
7). FGFRL1 affects chemoresistance of small-cell lung cancer by modulating the PI3K/Akt pathway via ENO1. JOURNAL OF CELLULAR AND MOLECULAR MEDICINE, 2020 (PubMed: 31957179) [IF=5.3]

Application: WB    Species: Human    Sample: SCLC cells

Figure 3 FGFRL1 induces chemoresistance of SCLC mainly by decreasing drug‐induced apoptosis and cell cycle arrest. A, B, Cell apoptosis and cell cycle arrest were evaluated by flow cytometric analysis in FGFRL1–down‐regulated SCLC cells after ADM exposure. C, D, Flow cytometric analysis of cell apoptosis and cell cycle arrest induced by ADM in FGFRL1‐overexpressing SCLC cells. E, F, Apoptosis‐related proteins were measured by Western blot following anticancer drug exposure in SCLC cells with down‐regulated or up‐regulated FGFRL1 expression. **P < .01; ***P < .001
8). SHMT2 promotes tumor growth through VEGF and MAPK signaling pathway in breast cancer. American Journal of Cancer Research, 2023 (PubMed: 35968337) [IF=5.3]
9). The MYC Paralog-PARP1 Axis as a Potential Therapeutic Target in MYC Paralog-Activated Small Cell Lung Cancer. Frontiers in Oncology, 2020 (PubMed: 33134168) [IF=4.7]

Application: IHC    Species: Human    Sample: tumor tissues

Figure 1 PARP1 mRNA tightly correlates with MYC paralog expression and is an independent prognostic marker of survival in patients with SCLC. (A) Kaplan–Meier analysis of the correlation between PARP1 expression and overall survival (OS, n = 77) and (B) progression-free survival (PFS, n=33). (C–E) Scatter plots of PARP1 mRNA relative to expression of MYC paralogs in SCLC primary tumors (n=81) (C), CCLE cell lines (n=50) (D), murine SCLC tumors (n=14) (E). (F) Representative images of IHC analysis of PARP1 and c-MYC in two independent cases. Scale bar, 100 μm. (G) Heat map showing the correlation between PARP1 and c-MYC in 17 paraffin-embedded SCLC tumor tissues. The heat map was depicted according to the IOD value of each IHC slides (red indicates c-MYC and PARP1 positive staining, green indicates negative staining). The significance analysis was performed by Student’s t test. (H–I) ChIP-qRT-PCR experiment indicating the direct binding of c-MYC and MYCN to the PARP1 promoter in DMS273 (H) and H526 (I) cells. (J) Western blot analysis showing the downregulated proteins in DMS53 and DMS273 cells upon c-MYC knockdown. (K) Western blot analysis showing the upregulated proteins in SHP77 cells with ectopic c-MYC overexpression. GAPDH was used as a loading control. BS, binding site.

Application: WB    Species: Human    Sample: tumor tissues

Figure 1 PARP1 mRNA tightly correlates with MYC paralog expression and is an independent prognostic marker of survival in patients with SCLC. (A) Kaplan–Meier analysis of the correlation between PARP1 expression and overall survival (OS, n = 77) and (B) progression-free survival (PFS, n=33). (C–E) Scatter plots of PARP1 mRNA relative to expression of MYC paralogs in SCLC primary tumors (n=81) (C), CCLE cell lines (n=50) (D), murine SCLC tumors (n=14) (E). (F) Representative images of IHC analysis of PARP1 and c-MYC in two independent cases. Scale bar, 100 μm. (G) Heat map showing the correlation between PARP1 and c-MYC in 17 paraffin-embedded SCLC tumor tissues. The heat map was depicted according to the IOD value of each IHC slides (red indicates c-MYC and PARP1 positive staining, green indicates negative staining). The significance analysis was performed by Student’s t test. (H–I) ChIP-qRT-PCR experiment indicating the direct binding of c-MYC and MYCN to the PARP1 promoter in DMS273 (H) and H526 (I) cells. (J) Western blot analysis showing the downregulated proteins in DMS53 and DMS273 cells upon c-MYC knockdown. (K) Western blot analysis showing the upregulated proteins in SHP77 cells with ectopic c-MYC overexpression. GAPDH was used as a loading control. BS, binding site.
10). TMEM97 is transcriptionally activated by YY1 and promotes colorectal cancer progression via the GSK-3β/β-catenin signaling pathway. Human Cell, 2022 (PubMed: 35907137) [IF=4.3]
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