PARP antibody - #BF0719

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Product: PARP antibody
Catalog: BF0719
Description: Mouse monoclonal antibody to PARP
Application: WB IHC
Reactivity: Human
Mol.Wt.: 113kDa; 113kD(Calculated).
Uniprot: P09874
RRID: AB_2846195

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

Product Info

Source:
Mouse
Application:
WB(1:500-1:2000), IHC(1:100-1:1000)
*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
Clonality:
Monoclonal [AFB17782]
Specificity:
PARP mouse monoclonal antibody detects endogenous levels of total PPAR.
RRID:
AB_2846195
Cite Format: Affinity Biosciences Cat# BF0719, RRID:AB_2846195.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), 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:

Purified recombinant fragment of human PPAR expressed in E. Coli.

Uniprot:

P09874(PARP1_HUMAN) >>Visit HPA database.

Gene(ID):
PARP1(142)
Sequence:
MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW

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). Crizotinib and Sunitinib Induce Hepatotoxicity and Mitochondrial Apoptosis in L02 Cells via ROS and Nrf2 Signaling Pathway. Frontiers in Pharmacology (PubMed: 33597889) [IF=5.6]

Application: WB    Species: Human    Sample: L02 cells

FIGURE 2 Crizotinib and sunitinib activated mitochondrial apoptosis in L02 cells. (A) After treatment with various concentrations of crizotinib or sunitinib for 48 h, the loss of MMP in cells was measured by JC-1 staining (n = 3). (B) The induction of apoptosis in L02 cells was determined by Annexin V/PI flow cytometry following treatment with increasing concentrations of crizotinib for 48 h, which was also employed to quantify the percentages of apoptotic and necrotic cells (n = 4). (C–E) The changes of PARP, c-caspase3, Bcl2, Bax and cytc protein expression were observed (n = 3). *p < 0.05, **p < 0.01 and ***p < 0.001 vs. control group.
2). Study on the biological mechanism of urolithin a on nasopharyngeal carcinoma in vitro. Pharmaceutical Biology (PubMed: 35952389) [IF=3.8]

Application: WB    Species: Human    Sample: CNE1 cells

Figure 7. UroA induced apoptosis maybe involved in ROS-mediated mitochondrial apoptosis pathway. (A) Western blot detects the expression of apoptosis-related proteins. Data are shown as mean ± SD for three independent experiments, *p < 0.05. **p < 0.01 and ***p < 0.001. (B) Intracellular ROS levels were measured by fluorescence microscope with DCFH-DA staining. (C) Western blot was used to detect the effects of reactive oxygen species specific inhibitor (NAC) on UroA-induced apoptosis in CNE1 and CNE2 cells. Data are shown as mean ± SD for three independent experiments, *p < 0.05.**p < 0.01 and ***p < 0.001.
3). Crosstalk between oxidative stress, autophagy and apoptosis in Hemoporfin Photodynamic Therapy treated human umbilical vein endothelial cells. Photodiagnosis and Photodynamic Therapy (PubMed: 33307232) [IF=3.3]

Application: WB    Species: Human    Sample: human umbilical vein endothelial cells (HUVECs)

Figure 4. Crosstalk between oxidization, autophagy and apoptosis in HUVECs after HMME-PDT (A) HUVECs were pretreated for 2h with 10 mM 3-MA, 20μM Z-VAD-FMK, or 10 mM NAC, and then treated with 5μg/ml HMME and light dose of 2 J/cm2 . Cell viability was detected by CCK8 assay 24h after HMME-PDT. ** p<0.01. (B) Autophagosome formation was observed in HUVECs 6h after HMME-PDT. Scale bar= 25μm. (C) The number of early autophagosomes (yellow puncta) per cell was calculated, and more than 10 cells were quantified for each condition. ** p<0.01. (D) TUNEL staining of HUVECs was performed 24h after HMME-PDT. Scale bar=100μm. (E) Apoptosis ratio Journal Pre-proof was calculated according to the TUNEL staining of HUVECs. ** p<0.01. (F) Western blotting analysis was used to measure the expression levels of Cytochrome C, Cleaved Caspase 3, PARP, Cleaved PARP, Beclin 1, LC3, and β-actin in HUVECs 24h after HMME-PDT

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