PARP1 Recombinant Monoclonal Antibody

Code: CSB-RA258431A0HU

Rate （N/A）
Review （0）

Size:

50μl100μl

US$210

Quantity:

Species Reactivity: Human

Application: ELISA, IHC

Send an Inquiry

Start an on-line Chat

Online ordering is currently available for U.S. customers only. For orders outside the U.S., please kindly submit an inquiry or start a chat with us.

Product Details
Related Products
Customer Reviews and Q&A
Target Background

Product Details

Uniprot NO.

P09874

Target Names

PARP1

Alternative Names

Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (NAD(+) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1), PARP1, ADPRT PPOL

Species Reactivity

Human

Immunogen

A synthesized peptide derived from human Cleaved PARP

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

5H8

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Scope Application

ELISA Protocol Immunohistochemistry (IHC) Protocol

Recommended Dilution

Application	Recommended Dilution
IHC	1:50-1:200

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Datasheet & COA

Antibody FAQs

Images

IHC image of CSB-RA258431A0HU diluted at 1:100 and staining in paraffin-embedded human lung cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4℃ overnight. The primary is detected by a Goat anti-rabbit IgG polymer labeled by HRP and visualized using 0.05% DAB.

Description

PARP1 serves as a critical enzyme in the cellular DNA damage response, catalyzing the addition of poly(ADP-ribose) chains to target proteins following genotoxic stress. This post-translational modification recruits repair machinery to sites of DNA breaks and plays a central role in maintaining genomic integrity. Notably, PARP1 cleavage by caspases during apoptosis has become a widely used marker for programmed cell death, making antibodies that recognize cleaved PARP1 particularly valuable for researchers studying cell death pathways, cancer biology, and therapeutic responses.

This recombinant monoclonal antibody, generated against a synthetic peptide derived from human cleaved PARP, offers the consistency and reproducibility that demanding experimental workflows require. Because the antibody sequence is defined and expressed recombinantly, you can expect uniform performance across different lots, eliminating the variability that can complicate long-term studies or multi-site collaborations. The rabbit IgG format, purified by affinity chromatography, ensures high specificity for your target.

Validation in immunohistochemistry demonstrates reliable performance in formalin-fixed, paraffin-embedded human lung cancer tissue, with recommended dilutions ranging from 1:50 to 1:200. The staining protocol, optimized using citrate buffer antigen retrieval and HRP-polymer detection, provides a solid starting point for your own tissue studies. Additional compatibility with ELISA extends its utility for quantitative applications.

Whether you are investigating apoptotic signaling in tumor samples, evaluating responses to DNA-damaging agents, or exploring PARP1's emerging roles in metabolism and epigenetic regulation, this antibody provides a dependable tool for advancing your research into this therapeutically important target.

Customer Reviews and Q&A

■ Customer Reviews

Submit a Review here

Target Background

Function(From Uniprot)

Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate, serine 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. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1. Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP1 active site. Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. 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, thereby promoting decompaction of chromatin and the recruitment of repair factors 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. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. 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. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and EEF1A1. 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.

Gene References into Functions

elevated expression of PARP-1 mRNA and miR-223, with a reduction of PARP-1 protein level and enzyme activity in colonic tissue of pediatric patients with Crohn's disease PMID:30299179
miR-7-5p reduced energy consumption via inhibiting PARP-1 expression, and miR-7-5p increased energy generation by suppressing the expression of Bcl-2. PMID:30219819
Study finds that PARP1 mutations caused a distinct set of drug sensitivities when compared to other known forms of PARPi resistance (loss of REV7 (MAD2L2) or TP53BP1, or BRCA1 reversion mutants), suggesting that knowledge of the molecular mechanism of resistance in individual patients could inform decisions on further treatment. PMID:29748565
Results suggest that RNF168 acts as a counterpart of PARP1 in DDR and regulates the HR/NHEJ repair processes through the ubiquitination of PARP1. PMID:30037213
two-step mechanism activates and then stabilizes PARP-1 on a DNA break, indicating that PARP-1 allostery influences persistence on DNA damage, with important implications for PARP inhibitors that engage the NAD(+) binding site PMID:29487285
PARP-1, via manipulating the binding of NF-kB/AP-1 at the MMP-9 promoter, regulates MMP-9 expression, which helps maintain mitochondrial homeostasis. PMID:28478229
Cell proliferation determines PARP1 transcription and production of electrophiles. PARP1 contributes to cell protection against electrophiles. PARP1 controls transcription of redox-sensitive kinases, antioxidants and detoxifying enzymes. [review] PMID:29886395
interactive domains between Ets-1 and PARP-1 have been mapped to the C-terminal region of Ets-1 and the BRCA1 carboxy-terminal (BRCT) domain of PARP-1 PMID:29912634
depletion of NOX1 and NOX4 partially rescued the growth inhibition of PARP1-deficient tumor xenografts. Our findings suggest that in addition to compromising the repair of DNA damage, PARP inhibition or depletion may exert extra antitumor effect by elevating oxidative stress in ovarian cancer cells PMID:29684820
CDK4/6 inhibitors also lead to accumulation of DNA damage by repressing PARP1 in oxidatively stressed cells. Thus, CDK4/6 inhibitors sensitize G1-arrested cells to anticancer drugs, since these cells require PARP1-OGG1 functional interaction for cell survival PMID:29306194
Low PARP expression is associated with mouth Cancer. PMID:30275188
The dysfunction of PARP1 in esophageal epithelial cells increases the levels of ROS and oxidative DNA damage in Barrett's esophagus. PMID:29531462
results suggest that PARP-1 overexpression may define an important risk factor in non-M3 AML patients and PARP-1 is a potential therapeutic target for AML treatment PMID:29812960
polymorphism of PARP-1 gene is more likely responsible for development of GD in Chinese individuals PMID:28177666
In response to DNA damage, activated and auto-poly-ADP-ribosylated PARP1 dissociates from HSF1-PARP13, and redistributes to DNA lesions and DNA damage-inducible gene loci. PMID:29158484
Results show that Rpp29 and Rpp21 bind poly ADP-ribose moieties and are recruited to DNA damage sites in a PARP1-dependent manner. PMID:28432356
PARP1 inhibitor also suppressed the aldosterone secretion in response to the angiotensin II. Together, these results suggest PARP1 is a prime coregulator for Nurr1. PMID:29738496
Here, we show that PARP1 and host insulator protein CTCF colocalize at specific sites throughout the EBV genome and provide evidence to suggest that PARP1 acts to stabilize CTCF binding and maintain the open chromatin landscape at the active Cp promoter during type III latency. Further, PARP1 activity is important in maintaining latency type-specific viral gene expression. PMID:29976663
Our findings showed that PARP-1 polymorphisms are involved in the development of glioma in Chinese individuals. PMID:28777431
Our results indicated that PARP1-siRNA can suppress the growth and invasion capacity of prostate cancer cells, thereby suggesting that PARP1-siRNA, which is different from PARP inhibitors , may provide a potential treatment method for prostate cancer . PMID:29393407
findings reveal PARP-1 as a double-edged sword in colorectal carcinogenesis, which suppresses tumor initiation following DNA alkylation in a MGMT-dependent manner, but promotes inflammation-driven tumor progression. PMID:29632181
data indicate that RNF20 and PARP1 are synthetic lethal interactors PMID:28462496
High PARP1 expression is associated with colonic neoplasms. PMID:29590171
On DNA damage, CIRBP temporarily accumulates at the damaged regions and is poly(ADP ribosyl)ated by poly(ADP ribose) polymerase-1 (PARP-1). PMID:29432179
The study suggests that PARP-1 polymorphisms are involved in the development of SCI in Chinese individuals. Thus, PARP-1 polymorphisms can be considered as one of the potential risk factors for developing SCI. PMID:29255350
this study identifies the importance of TDP1 as a novel determinant of response to CNDAC across various cancer types (especially non-small cell lung cancers), and demonstrates the differential involvement of BRCA2, PARP1, and TDP1 in the cellular responses to CNDAC, AraC, and CPT PMID:28802254
Variations in potential miRNA-binding target sites in the 3' UTR of PARP1 gene may modulate colorectal cancer risk and prognosis after therapy. PMID:29048575
Three-locus model of gene-gene interactions OGG1 (rs1052133) * ADPRT (rs1136410) * XRCC4 (rs6869366) was associated with high genotoxic risk in coal miners. PMID:28992182
Observations suggest that IER5 is a novel regulator of the non-homologous end-joining pathway pathway for DNA double-strand breaks repair, possibly through its interaction with PARP1 and Ku70. PMID:29104487
This study identified the involvement of two SNPs of PARP-1 (C410T and G1672A) in development of acute renal injury among Chinese diabetic patients. PMID:29238179
Studies indicate that post-translational modifications (PTMs) such as phosphorylation, acetylation, and methylation are crucial for the regulation of PARP1 activity, and dysregulation of modifications on PARP1 is observed in cancer [Review]. PMID:28930534
Poly(ADP-ribose) polymerase-1 (PARP1) interacts with xeroderma pigmentosum, complementation group C protein (XPC) in the nucleoplasmic and chromatin fractions in UV irradiated HEK293 cells. PMID:28760956
The phosphorylation level of p38 was upregulated by MA1 treatment, and the inhibitor of p38, SB203580, attenuated the MA1-induced p38 phosphorylation as well as caspase3 and PARP activation. These results indicate that MA1 treatment alters invasive and oncogenic phenotypes of human colorectal cancer cells through the stimulation of the p38 signaling pathway PMID:28713983
this study demonstrates that PARP inhibition protects mitochondria and reduces ROS production via PARP-1-ATF4-MKP-1-MAPK retrograde pathway PMID:28457938
Arsenite-loaded nanoparticles inhibit PARP-1 to overcome multidrug resistance in hepatocellular carcinoma cells. PMID:27484730
NR1D1 interacted with poly(ADP-ribose) polymerase 1 (PARP1) and subsequently inhibited catalytic activity of PARP1. PMID:28599788
IGH/MYC-positive Burkitt lymphoma/leukemia cells have decreased BRCA2 and are sensitive to PARP1 inhibition alone or in combination with other chemotherapies. This study postulates that IGH/MYC-induced BRCA2 deficiency may predispose Burkitt lymphoma cells to synthetic lethality triggered by PARP1 inhibitors. PMID:28634224
Our study demonstrates a cross-talk between PARPi and tumor-associated immunosuppression and provides evidence to support the combination of PARPi and PD-L1 or PD-1 immune checkpoint blockade as a potential therapeutic approach to treat breast cancer PMID:28167507
PARP1 expression was increased in GBM at both mRNA and protein levels. increased PARP1 levels show positive correlation with increasing tumour grades in gliomas Higher PARP1 mRNA expression levels were associated with ATRX and TP53 mutations. PMID:28654422
Existence of a kinase-independent role of nuclear RIPK1 in the regulation of PARP1. PMID:28993228
The observed incomplete sister chromatid disjunction may be due to the accumulation of unreplicated DNA during mitosis in CDA-deficient cells, as reflected in the changes in centromeric DNA structure associated with the decrease in basal PARP-1 activity. PMID:28463527
Studied role of PARP1 regulation and senescence by melatonin. PMID:28247536
Report a requirement for PARP2 in stabilizing replication forks that encounter base excision repair (BER) intermediates through Fbh1-dependent regulation of Rad51. Whereas PARP2 is dispensable for tolerance of cells to single stranded breaks or homologous recombination dysfunction, it is redundant with PARP1 in BER. PMID:29467415
Potential high binding affinity compounds that are predicted by molecular simulations were then tested by in vitro methods. Computationally proposed compounds as PARP-1 inhibitors were confirmed by in vitro studies. In vitro results showed that compounds 7111620047 and 7119980926 have IC50 values of 0.56 and 63 muM against PARP-1 target, respectively PMID:27315035
The impairment of PARP-dependent DNA damage response (DDR) signaling due to mutations in the FUS nuclear localization sequence induces additional cytoplasmic FUS mislocalization which in turn results in neurodegeneration and FUS aggregate formation in amyotrophic lateral sclerosis. PMID:29362359
Septin4 is a novel essential factor involved in oxidative stress induced vascular endothelial cell injury by interacting with apoptosis-related protein PARP1. PMID:29366480
Data show that the mRNA level of poly(ADP-ribose) polymerase (PARP)-1 was significantly regulated by miR-216b. PMID:28281524
The Gene expression levels of PARP1 was robustly elevated in oligodendrocytes laser captured from BA10 and amygdala white matter of Major Depressive Disorder. PMID:28034960
PARP-1 activates prothrombin gene transcription and that the excessive prothrombin gene transcription induces des-gamma-carboxy prothrombin (DCP) production in DCP-producing hepatocellular carcinoma cells. PMID:28384634
Sodium arsenite induces S-nitrosation on PARP-1 zinc finger DNA binding domain by generating NO through iNOS activation, leading to zinc loss and inhibition of PARP-1 activity, thereby increasing retention of damaged DNA. PMID:27741521