Cleaved-PARP (Asp214) Antibody | Affinity Biosciences

Product:	Cleaved-PARP (Asp214) Antibody
Catalog:	AF7023
Description:	Rabbit polyclonal antibody to Cleaved-PARP (Asp214)
Application:	WB
Cited expt.:	WB
Reactivity:	Human, Mouse, Rat
Prediction:	Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.:	85kDa(cleaved), 115kDa(precursor); 113kD(Calculated).
Uniprot:	P09874
RRID:	AB_2835327

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Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific.

Size	Price	Inventory
50ul	$250	In stock
100ul	$350	In stock
200ul	$450	In stock

Lead Time: Same day delivery

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Related Downloads

MSDS

Data Sheet

COA

Protocols

WB Handbook

IHC Protocol

IF/ICC Protocol

Product Info

Source:

Rabbit

Application:

WB 1:500-1:2000
*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(83%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(83%), Xenopus(83%)

Clonality:

Polyclonal

Specificity:

Cleaved-PARP (Asp214) Antibody detects endogenous levels of fragment of activated PARP resulting from cleavage adjacent to Asp214.

RRID:

AB_2835327
Cite Format: Affinity Biosciences Cat# AF7023, RRID:AB_2835327.

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.Stable for 14 months from date of receipt. 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:

The antiserum was produced against synthesized peptide derived from human PARP.

Uniprot:

P09874(PARP1_HUMAN) >>Visit HPA database.

Gene(ID):

PARP1(142)

Description:

Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks.

Sequence:

P09874 PARP1_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

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

Rabbit

100

Xenopus

Zebrafish

Chicken

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

Research Backgrounds

P09874_PARP1_HUMAN

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.

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). Structure and in vitro antiproliferative activity against breast cancer cells of the cell-wall polysaccharide from the marine bacterium Kangiella japonica KMM 3899T. Carbohydrate polymers, 2024 (PubMed: 38876721) [IF=10.7]

2). Cell-cycle arrest and mitochondria-dependent apoptosis induction in T-47D cells by the capsular polysaccharide from the marine bacterium Kangiella japonica KMM 3897. Carbohydrate Polymers, 2023 (PubMed: 37659798) [IF=10.7]

3). AKAP8L enhances the stemness and chemoresistance of gastric cancer cells by stabilizing SCD1 mRNA. Cell Death & Disease, 2022 (PubMed: 36522343) [IF=8.1]

4). Metformin modified chitosan as a multi-functional adjuvant to enhance cisplatin-based tumor chemotherapy efficacy. International Journal of Biological Macromolecules, 2023 (PubMed: 36283555) [IF=7.7]

5). Quercetin induces autophagy via FOXO1-dependent pathways and autophagy suppression enhances quercetin-induced apoptosis in PASMCs in hypoxia. FREE RADICAL BIOLOGY AND MEDICINE, 2017 (PubMed: 27979659) [IF=7.1]

Application: WB Species: rat Sample:

6). Edaravone combined with dexamethasone exhibits synergic effects on attenuating smoke-induced inhalation lung injury in rats. Biomedicine & Pharmacotherapy, 2021 (PubMed: 34225014) [IF=6.9]

Application: WB Species: Rat Sample: lung tissues

Fig. 4. Effect of edaravone and/or dexamethasone on smoke-induced cell apoptosis.

7). Packaging cordycepin phycocyanin micelles for the inhibition of brain cancer. Journal of Materials Chemistry B, 2017 (PubMed: 32264358) [IF=6.1]

Application: WB Species: Mouse Sample: C6 cells

Fig. 4 Measured apoptosis and protein expression in C6 cells treated with (a) PBS, (b) Dextran, (c) Phycocyanin, (d) Cordycepin, (e) the Phycocyanin/Cordycepin mixture, or (f) Phy-Dex-Cord micelles for 24 h. (A) Trypan blue staining was used to observe cell morphology (Bar: 100 µm). (B) Apoptotic cells were detected with flow cytometry. Subcellular localization (C1) cleaved caspase-3 and (C2) cleaved PARP in C6 cells, as determined by Confocal laser scanning microscopy. (D1) Apoptosis-related protein, and (D2, D3) quantitative analysis of Bax, Bcl-2, p53, cleaved caspase-3, cleaved PARP, and PARP levels in C6 cells. Significant increase or decrease at labels (*) (p < 0.05), labels (**) (0.001< p < 0.01) and labels (***) p < 0.001, are identified in comparison with the Control group. (E) Cell counting determination of apoptotic rate with Trypan blue and statistical analysis of FCM results.

8). A Potent Protective Effect of Baicalein on Liver Injury by Regulating Mitochondria-Related Apoptosis. APOPTOSIS, 2020 (PubMed: 32409930) [IF=6.1]

Application: WB Species: human Sample: L02 cells

Fig. 4| Protective efect of baicalein on H2O2 induced hepatotoxicity. L02 cells were pre-treated with 100 μM H2O2 for 1 h, then co-incubated with 50 μM baicalein for 11 h. a Mitochondrial and apoptosis were stained with MitoTracker Red and TUNEL, respectively. b The percentage of cells underwent mitochondrial fssion and TUNEL positive cell. c The expression levels of apoptotic and autophagy related proteins were detected by western blotting and densitometry.

9). Carbamoylation at C-8 position of natural 3-arylcoumarin scaffold for the discovery of novel PARP-1 inhibitors with potent anticancer activity. European journal of medicinal chemistry, 2024 (PubMed: 39116535) [IF=6.0]

10). Berberine Prolongs Mouse Heart Allograft Survival by Activating T Cell Apoptosis via the Mitochondrial Pathway. Frontiers in Immunology, 2021 (PubMed: 33732240) [IF=5.7]

Application: WB Species: Mice Sample:

Figure 4 Phenotypic and functional characteristics of allograft-infiltrating CD4+ or CD8+ T cells. Allografts were recovered at POD 7, and POD 100 syngeneic grafts are shown for comparison. (A) (i) Immunofluorescent staining of CD4 (red), KI67 (green), and 4′,6-diamidino-2-phenylindole (DAPI, blue) in grafts. (ii) Immunofluorescent staining of CD8 (red), KI67 (green), and DAPI in grafts (Scale bar = 200 μm; original magnification: ×200). (B) Proportion and absolute number of graft-infiltrating (i) CD4+ T cells and their expression of (ii) KI67, and proportion and absolute number of graft-infiltrating (iii) CD8+ T cells and their expression of (iv) KI67 (n = 3 mice/group). (C) Proportion of (i) IFN-γ and (ii) cleaved-caspase-3 in graft-infiltrating CD3+ T cells (n = 3 mice/group). (D) (i) Cleaved-caspase-3 and cleaved-PARP protein expression in grafts. Myocardial cell apoptosis co-immunofluorescence staining and expression of (ii) cleaved-caspase-3 and (iii) cleaved-PARP (n = 3 mice/group). (E) Relative mRNA expression of IFN-γ, IL-6, IL-10, Foxp3, and FasL in grafts measured by qPCR (n = 3 mice/group). SPCs, spleen cells; LNCs, lymph node cells; POD, post-operative day. *p < 0.05, **p < 0.01, ***p < 0.001 compared to the normal saline-treated group.

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Cleaved-PARP (Asp214) Antibody - #AF7023