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Validated All-in-One™ qPCR Primer for PARP1(NM_001618.3) Search again
Product ID:
HQP003120
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ADPRT, ADPRT 1, ADPRT1, ARTD1, PARP, PARP-1, PARS, PPOL, Poly-PARP, pADPRT-1
Gene Description:
poly(ADP-ribose) polymerase 1
Target Gene Accession:
NM_001618.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a chromatin-associated enzyme, poly(ADP-ribosyl)transferase, which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, this enzyme may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes. [provided by RefSeq].
Gene References into function
- Here, we show that PARP activation reaction in vitro becomes acidic with release of protons during hydrolysis of beta-nicotinamide adenine dinucleotide
- PARP co-activates B-MYB through enhanced phosphorylation at cyclin/cdk2 sites
- PARP-1 degradation in etoposide-treated apoptotic cells may precede DNA cleavage.
- PARP expression in Ewing's sarcoma cells
- Escherichia coli shiga-like toxins induce apoptosis and cleavage of poly(ADP-ribose) polymerase via in vitro activation of caspases
- TRAIL treatment did not result in PARP cleavage.
- PARP immunoreactivity is increased 3-fold in spinal cord tissues of sporadic amyotrophic lateral sclerosis (sALS) patients compared with non-neurological disease controls, demonstrating a role of glial alterations in sALS pathogenesis.
- Inhibition of BRCA1 via overexpressing the RHA fragment coincides with a reduction in PARP-1 protein expression. PARP-1 is identified as a downstream effector of BRCA1 function in the maintenance of genomic stability.
- Poly(ADP-ribose) polymerase activation and changes in Bax protein expression associated with extracellular ATP-mediated apoptosis in human embryonic kidney 293-P2X7 cells.
- PARP-1 haplotypes play a role in susceptibility to rheumatoid arthritis.
- study establishes poly(ADP-ribose) polymerase-1 as a critical regulator of the protein p53 response to DNA damage
- Translocation of this protein was used to monitor the partial purification of the active components(s) from both human T cell and yeast extracts.
- PARP-1 does not play a major role in catalysis of DNA damage processing via either base excision repair pathway.
- polyADP ribosyl transferase level is linked with the oxidoreduction reactions seen in Fanconi anemia
- examination of binding of central and carboxy-terminal regions p53 protein
- centenarian subjects display low MTmRNA, good zinc ion bioavailability, satisfactory NK cell activity and higher capacity of PARP-1 in base excision DNA-repair.
- in the peripheral blood, appears to be present at higher rates in COPD patients than in healthy age-matched controls
- PARP-1 and p21 could cooperate in regulating the functions of PCNA during DNA replication/repair.
- PARP-1 acts synergistically with p300 and plays an essential regulatory role in NF-kappaB-dependent gene expression
- reduced blood flow and subsequent ischemic damages in leiomyoma could be responsible for PARP overexpression and PAR accumulation, clinical response, and tumor degeneration caused by leuprorelin treatment.
- cellular poly(ADP-ribose) polymerase 1 (PARP-1) and Ste20-like kinase hKFC interact with the serine/threonine-rich region of gamma-2 herpesvirus replication and transcription activator (RTA)
- interaction of ADPRT and WRN resulting in ADP-ribosylation of the WRN protein; results imply that WRN is involved in DNA replication and in DNA repair
- the WRN/PARP-1 complex plays a key role in the cellular response to oxidative stress and alkylating agents, suggesting a role for these proteins in the base excision DNA repair pathway
- nitric oxide and reactive nitrogen oxide species inhibit PARP
- PARP-1 and PARP-2 act as positive regulators of genomic stability in eukaryotic cells by counteracting topoisomerase I-induced DNA damage
- activity of E. coli topoisomerase I is specifically associated with poly(ADP-ribose) polymerase-1
- Data show that poly(ADP-ribose) polymerase 1 (PARP-1) is expressed during fetal development and undergoes complex developmental changes in expression, and that inhibition of PARP-1 activity differentially affects expression of surfactant proteins.
- PARP-immunoreactivity is increased in reactive astrocytes in the central nervous system of SOD1(G93A) transgenic mice, suggesting a role for PARP-expressing astrocytes in the pathogenesis and progress of amyotrophic lateral sclerosis.
- PARP-1 in biopsy specimens from aged donors may be a useful predictive factor for renal graft function.
- identify TIN2 as a PARP modulator in the TRF1 complex
- function for the automodification reaction is to regulate the interaction between PARP-1 and Topo I, and consequently, the Topo I activity, in response to DNA damage.
- Over-activation of PARP can contribute to the pathomechanism of the disease-specific lesion of the neurons in the substantia nigra in Parkinson disease.
- required for efficient HIV-1 replication in human cells
- Inhibition of PARP-1 and DNA-dependent protein kinase id a powerful strategy for tumor radiosensitization.
- Poly(ADP-ribose) polymerase 1 inactivates the catalytic activities of the Werner syndrome protein.
- ICAM-1, VCAM-1, E-selectin and interleukin-6 expression are enhanced by glucose and regulated by poly(ADP-ribose) polymerase in human umbilical endothelial cells
- PARP1 bound directly to a specific region within the Kaposi's sarcoma-associated herpesvirus (KSHV) terminal repeat sequence
- role for PARP in the onset and progression of cardiac hypertrophy; some events related to cardiac hypertrophy growth and progression to heart failure are mediated by a PARP-dependent mechanism.
- Increased expression of poly(ADP-ribose) polymerase is associated with hepatocellular carcinoma
- Data provide novel insight into the function of poly(ADP-ribose) polymerase-1 (PARP-1) in inflammation and ischemia-related pathophysiologies.
- poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III utilize an alternative route for DNA double-strand breaks rejoining
- Upregulated by cetrorelix in cultured leiomyoma cells.
- normal cells but not pituitary tumor cells are able to sufficiently activate PARP to prevent rapid cell death
- PCNA expression induces apoptosis by up-regulating cleaved caspase-3 and PARP expression and down-regulating Bcl-2 protein expression in leiomyoma cells.
- PARP-1 functions both as a structural component of chromatin and a modulator of chromatin structure through its intrinsic enzymatic activity.
- The association of different NACP-Rep1 alleles with Parkinson's disease may be mediated, in part, by the effect of PARP-1 on SNCA expression.
- PARP-1 poly(ADP-ribosyl)ation is a terminal event in the apoptotic response that occurs in response to DNA fragmentation and directly influences DFF40 activity
- PARP-1 activation and a PARP-1-dependent, caspase-independent, nuclear translocation of apoptosis inducing factor contribute to apoptotic cerebral endothelial cell death after ischemia-reperfusion
- Interplay between APE1, DNA polymerase beta and poly(ADP-ribose) polymerase-1 during base excision repair.
- the structural features of non-B form DNA co-factors are important for PARP-1 catalysis activated by undamaged DNA
- PARP-1 is involved in expression of ERBB2 in concert with NF-kappaB, which might be associated with proliferation of rheumatoid arthritis synovial cells.
- poly(ADP-ribose) polymerase-1 in the cell nucleus rapidly triggers mitochondrial dysfunction
- PARP-1 expression appeared to be co-ordinated with that of Sp1 and Sp3 in primary cultured cells, suggesting that PARP-1 may play some important functions during the proliferative burst that characterizes wound healing.
- PARP-1 binding to DNA single-strand breaks or repair intermediates plays a protective role when repair is limited
- Anti-La/SSB antibodies were accompanied by significant increased leukocytes (P < .02). PARP cleavage (85 kDa) in nuclei was preferentially observed in cases with nuclear targeting autoantibodies
- Data show that PARP-1 differs from other cruciform-binding proteins by binding to hairpin tips rather than to junctions, and that PARP-1 can interact with the gene regulatory sequences by binding to the promoter-localized cruciforms.
- PARP-1 plays an important role in acute tubular necrosis and recovery of renal function and is related to the extent and severity of ATN and to the renal allograft function.
- PARP-1-mRNA expression was increased in mononuclear cells from all diabetic patients. Could therefore be responsible for the abnormal inflammation and infection responses in diabetes.
- expression of PARP-1 was closely associated with the accumulation of beta-catenin and with the undifferentiated status of intestinal epithelial cells; PARP-1 may participate in early colorectal carcinogenesis
- These results suggest that PARP-1 is required for HIV-1 integration near the centromere region both in human and murine cells.
- results provide the first evidence that PARP-1 haplotypes are related with coeliac disease susceptibility
- results implicate CSB in the PARP-1 poly(ADP-ribosyl)ation response after oxidative stress and thus suggest a novel role of CSB in the cellular response to oxidative damage
- PARP inhibition-induced Akt activation is dominantly responsible for the cytoprotection in oxidative stress
- Although PARP-1 appears not to be required for homologous recombination itself, it regulates the process through its involvement in the repair of DNA single-strand breaks [review]
- The specific inhibition of Aurora-B kinase activity by PARP-1 contributes to the physiological response to DNA damage.
- PARP activation and the concomitant reduction of Sir2alpha activity in failing hearts regulate the post-translational acetylation of p53
- nucleolin and poly[ADP-ribosyl] transferase have roles in drug resistance
- Data show that the amino-terminal DNA-binding domain of human PARP-1 binds a 5'-recessed DNA end cooperatively with a stoichiometry of two proteins per DNA molecule.
- Data show that one mechanism through which oxidative stress or TNF-alpha mediates cell death is activation of TRPM2, resulting in increased internal calcium, followed by caspase activation and PARP cleavage.
- Down-regulation of PARP1 in TUR leukemia cells restores transcriptional responsiveness for differentiation and cell cycle arrest.
- ADPRT Val762Ala and XRCC1 Arg399Gln polymorphisms may not play a role in the etiology of breast cancer.
- Data show that polynucleotide kinase is associated with the PARP-1-dependent end-joining pathway, and show functional parallels between the PARP-1 and DNA-PK-dependent end-joining processes.
- PARP-1 expression and cold ischemia duration in kidney biopsies with acute tubular necrosis predicted the short-term delay in total recovery of renal function and serum creatinine in the first month.
- the APE1 Glu variant, but not an ADPRT variant, may have an effect or interact with XRCC1 in the etiology of cutaneous melanoma or in linkage disequilibrium
- These results suggest that PARP1 phosphorylation by ERK1/2 is required for maximal PARP-1 activation after DNA damage.
- AIF-mediated cell death is regulated by the functional interplay of SIRT1 and PARP-1 in response to DNA damage
- The ADPRT and XRCC1 polymorphisms confer host susceptibility to GCA, which might result from reduced ADPRT-XRCC1 interaction and attenuated base excision repair capacity.
- Ca(2+) appears to be an important co-factor in PARP-1 hyperactivation after reactive oxygen species-induced DNA damage, which alters cellular metabolism and DNA repair
- The current data provide evidence of oxidative stress and PARP activation in human heart failure.
- PARP-1 and Hsp90 bind to TonEBP; PARP-1 expression reduces TonEBP transcriptional activity and the activity of its transactivating domain and Hsp90 enhances those activities.
- Upon heat shock, the Hsp70.1 promoter-bound PARP-1 is released to activate transcription through ADP-ribosylation of other Hsp70.1 promoter-bound proteins.
- E4orf6 disrupts cellular DSBR signaling by inhibiting PP2A, leading to prolonged H2AX phosphorylation, hyperactivation of PARP, and AIF translocation to the nucleus.
- poly(ADP-ribose)polymerase-1 and Ku70/Ku80 are transcriptional regulators of S100A9 gene expression
- These results represent the first direct demonstration of PARP activation in human myocardial infarction.
- PARP-1-410 and PARP-1-1672 haplotypes were associated with an increased risk for AD and, in addition, PARP-1 haplotypes increased the risk of AD by interaction with the IL-1A -889 allele 2.
- These data imply that PARP activation following exposure to ionizing radiation is enhanced through EGFR-ERK signaling.
- retrodifferentiation of growth-arrested U937 monocytic cells requires proteasomal protein degradation and activity of PARP-1
- depending on its state of phosphorylation, NMNAT-1 binds to activated, automodifying PARP-1 and thereby amplifies poly(ADP-ribosyl)ation
- A protective effect against PD was found for heterozygosity at (-410) (OR 0.44) and (CA)n microsatellite (OR 0.53) polymorphisms, and heterozygosity at (-1672) polymorphism delayed by 4 years on the onset age of PD.
- This study indicates that PARP expression is frequently upregulated in ovarian serous carcinomas, related with MIB-1 LIs and p53 expression, and may serve as a marker of aggressive behavior with prognostic value.
- physical interaction between the major DSB signaling kinase, ATM and poly(ADP-ribosyl)ation by PARP-1, a key enzyme of chromatin remodeling.
- while PARP-1 is needed in the response of ATM to gamma irradiation, the inhibition of PARP induces DNA double strand breaks
- cells from old subjects show a constitutive expression level of both parp 1 and parp 2 genes reduced by a half
- SET and PARP1 remove DEK from chromatin to permit access by the transcription machinery
- In diabetic patients, FPG-sensitive DNA strand breaks correlated positively with PARP gene expression, PARP activity and NFkappaB binding activity.
- PARG is identified as a novel and critical component of single-strand break repair that accelerates this process in concert with PARP-1.
- Genetic variants of PARP-1 may contribute to breast cancerogenesis; PARP-1 htSNP c.852T>C (Ala284Ala) may influence hormonal therapy of breast cancer.
- PARP activity has an important role in providing the retinal pigment epithelium with the high oxidative tolerance required for this cell type to survive the constant reactive oxygen species attack in vivo for several decades.
- Results identified nuclear protein poly (ADP-ribose) polymerase family, member 1 (PARP1) as a nuclear protein binding to the SMARCB1 promoter and showed that the -228 SNP significantly altered PARP1 binding affinity.
- molecular evidence presented that the differential apoptotic cell-induced IL-10 gene expression in individuals with the GCC or ATA promoter haplotypes is determined at the level of transcription mediated by PARP-1
- These results show that the DNA binding domain and catalytic domain cooperate to regulate chromatin structure and transcription, providing mechanistic insights into how these domains contribute to the chromatin-dependent functions of PARP-1.
- The results of this study indicate that specific flavonoids have PARP-1-inhibiting activity and that this could play a role in the anti-inflammatory activity of these compounds.
- Kidney transplant events including ischemia were associated with the highest PARP-1 expression and worse allograft renal function.
- AG490 enhances UCN-01-induced cytotoxicity in p53 defective cell lines by suppression of BAD phosphorylation and induction of BAX and PARP cleavage
- detailed mutation and haplotype tagging analysis of the ADPRT gene with regard to breast cancer
- poly(ADP-ribose) polymerase has a role in excision repair of single-strand breaks; review of its inhibitors and their use in cancer therapy [review]
- Poly(ADP-ribose) polymerase 1 (PARP1) is a nuclear enzyme that is rapidly activated by DNA strand breaks and signals the presence of DNA lesions by attaching ADP-ribose units to chromatin-associated proteins.
- Results suggest that the PARP1 gene is involved in the pathogenesis of diabetic neuropathy in a Russian population.
- These results highlight a new role of the PARP-1 protein on the synapsis of DSBs and could explain why the PARP-1 NHEJ pathway is strongly dependent on the DSBs microhomology sequence.
- demonstrate using spectroscopic and crystallographic analysis that human PARP-1 has a third zinc-binding domain
- The nuclear binding site of PARP-1 is Topo I, and is identified as a critical "switchpoint" indicating the nuclear element that connects OXPHOS with mRNA synthesis in real time.
- These data point to PARP-1 and poly(ADP-ribosyl)ation as a novel regulatory mechanism of NFAT at nuclear level.
- caspase-3 activation by RSVL is required for PARP degradation and induction of apoptosis
- Our results indicate that nicotinamide treatment attenuates p21WAF1 expression through Sp1 downregulation, and suggest a possible involvement of nicotinamide metabolism in cellular gene expression.
- histone H1 & PARP-1 exhibit a reciprocal pattern of chromatin binding at many RNA polymerase II-transcribed promoters; study showed PARP-1 acts to exclude H1 from a subset of PARP-1-stimulated promoters
- These results give the first direct demonstration that PEDF might represent a target for PARP inhibition treatment and the effects of PEDF on endothelial cells growth are context dependent.
- These findings strengthen the importance of the role of PARP1 as a transcriptional coactivator of HIF-1-dependent gene expression during tumor progression.
- hPARP-1 gets catalytically activated upon binding to G-quadruplexes localized at the c-kit promoter and human telomere regions
- Determination of Poly (ADP-ribose) polymerase (PARP) homologues in human ejaculated sperm and its correlation with sperm maturation.
- PARP activity determines the fate of HeLa cells by regulating the level of ATP after treatment with MNNG
- presence of heat-labile sites has a substantial impact on DSB induction and DSB rejoining rates measured by pulsed-field gel electrophoresis, and heat-labile sites repair is independent of DNA-PKcs, XRCC1 and PARP
- TFII-I, PARP1, and SFPQ proteins, each previously implicated in gene regulation, form a complex controlling transcription of DYX1C1. Allelic differences in the promoter or 5'UTR of DYX1C1 may affect factor binding and thus regulation of the gene.
- human poly(ADP-ribose) polymerase-1 domain C is important for enzyme activity and contains a novel zinc-ribbon motif
- As PAR-modified protein concentration correlated with age and male sex, developmental and sex-dependent roles for PARP after TBI are implicated.
- during conditions of oxidative stress in lymphocytes, TRPM2 acts as a downstream effector of the PARP/poly(ADP-ribose) glycohydrolase pathway through PARP-dependent formation of ADP-ribose.
- Low concentration of arsenite exacerbates UVR-induced DNA strand breaks by inhibiting PARP-1 activity.
- PARP-1 is the PARP family member playing the most prominent role in the upregulation of c-Fos and c-Myc during G0-G1 transition.
- The histone subcode: poly(ADP-ribose) polymerase-1 (Parp-1) and Parp-2 control cell differentiation by regulating the transcriptional intermediary factor TIF1beta and the heterochromatin protein HP1alpha
- Vitamin A depletion causes oxidative stress, mitochondrial dysfunction, and PARP-1-dependent energy deprivation
- Results suggest that PARP1 behaves as an important negative co-factor involved in the regulation of Pax8-dependent gene expression.
- ILK silencing inhibited binding of PARP-1 to SIRE
- This variant can interact with ADPRT-762Ala variant to further substantially increase susceptibility to the disease and regional LN metastasis.
- The results of our study have shown that KU-0059436 increases radiosensitivity in a replication-dependent manner that is enhanced by fractionation.
- Parp-1 down-regulates BRCA2 expression through an interaction with a repression region of the BRCA2 promoter
- Data show that overexpressed PARP-1 promotes PARP-1/NF-kappaB/DNA complex formation, enhancing the expression of TNF-alpha and IL-6 in circulating mononuclear cells of unstable angina patients.
- Drugs inhibiting PARP-1 may represent valuable tools for pharmacological treatment of stroke patients.
- The expression of human PARP-1 restores fork slowing in PARP-1(-/-) DT40 cells. PARP-1 affects SSB repair, homologous recombination (HR), and nonhomologous end joining.
- The PARP1 SNP A762V showed a significant association with glioma risk.