Recombinant Human Poly [Adp-Ribose] Polymerase 1 (PARP1) Protein (His-GST)

Name: Recombinant Human Poly [Adp-Ribose] Polymerase 1 (PARP1) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-07488P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Poly [Adp-Ribose] Polymerase 1 (PARP1) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P09874
Target Symbol	PARP1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	KTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEH
Expression Range	324-541aa
Protein Length	Partial
Mol. Weight	55.2 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Nucleus. Nucleus, nucleolus. Chromosome.
Database References	HGNC: 270 OMIM: 173870 KEGG: hsa:142 STRING: 9606.ENSP00000355759 UniGene: 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

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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