Recombinant Human Poly [Adp-Ribose] Polymerase 2 (PARP2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00826P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Poly [Adp-Ribose] Polymerase 2 (PARP2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00826P
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Product Overview

Description Recombinant Human Poly [Adp-Ribose] Polymerase 2 (PARP2) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q9UGN5
Target Symbol PARP2
Species Homo sapiens (Human)
Expression System E.coli
Tag C-10His
Target Protein Sequence QLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW
Expression Range 233-583aa
Protein Length Partial
Mol. Weight 41.3 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 or serine 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. 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 PARP2 active site. PARP2 initiates the repair of double-strand 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 proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex.
Subcellular Location Nucleus. Chromosome.
Database References
Tissue Specificity Widely expressed, mainly in actively dividing tissues. The highest levels are in the brain, heart, pancreas, skeletal muscle and testis; also detected in kidney, liver, lung, placenta, ovary and spleen; levels are low in leukocytes, colon, small intestine

Gene Functions References

  1. PARP2 is preferentially activated by poly(ADP-ribose) (PAR) and subsequently catalyzes branched PAR chain synthesis. PMID: 30104678
  2. data further suggest that ARTD2 would function in double strand break repair as a dimeric module, while in single strand break repair it would function as a monomer. PMID: 27708353
  3. 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
  4. PARP2 specifically limits the accumulation of the resection barrier factor 53BP1 at DNA damage sites, allowing efficient CtIP-dependent DNA end-resection PMID: 29036662
  5. either PARP1 or PARP2 are sufficient for near-normal XRCC1 recruitment at oxidative single-strand breaks PMID: 27965414
  6. Studies indicate that poly(ADP-ribose) polymerase 2 (PARP2) is involved in the differentiation of several cell types, including erythrocytes, T cells and adipocytes. PMID: 27087568
  7. Findings indicate that Increased poly(ADP-ribose) polymerase-2 (PARP-2) expression and loss of micrRNA miR-149 expression are involved in the pathogenesis of hepatocellular carcinomas (HCC) and are poor prognosis factors in patients with HCC. PMID: 27300349
  8. Data show that E7449 represents a dual Poly(ADP-ribose) Polymerase 1/2 and tankyrase 1/2 inhibitor which has the advantage of targeting Wnt/beta-catenin signaling addicted tumors. PMID: 26513298
  9. The initial affinity between the PARP1, PARP2 and the DNA damaged site appears to influence both the size of the Poly(ADP-Ribose) synthesized and the time of residence of PARylated PARP1 and PARP2 on DNA damages. PMID: 26673720
  10. Our data suggest for the first time that a SNP in PARP2, rs878156, may together with other genetic variants modulate cancer specific survival in breast cancer patients depending on chemotherapy PMID: 26674097
  11. Our study differentiates the functions of PARP-2 domains from those of PARP-1, the other major DDR-PARP, and highlights the specialization of the multi-domain architectures of DDR-PARPs. PMID: 26704974
  12. Interaction of PARP-2 with AP site containing DNA PMID: 25724268
  13. Identification of ADP-ribosylation sites in PARP2 and the determination of the extent ofpoly(ADP-ribosyl)ated residues in this protein was performed. PMID: 25800440
  14. Nuclear Smad function is negatively regulated by PARP-1 that is assisted by PARP-2 and positively regulated by PARG during the course of TGFB signaling. PMID: 25133494
  15. the depletion of PARP-2 leads to lower HDL levels which represent a risk factor to cardiovascular diseases. PMID: 24365238
  16. these findings propose a novel mechanism of PARP-2 in transcriptional regulation involving specific protein-protein interactions and highlight the importance of PARP-2 in the regulation of cell cycle progression. PMID: 23291187
  17. PARP-1 (but not PARP-2) poly(ADP) ribosylates Snail1, both in vivo and in vitro, and interacts with Snail1, an association that is sensitive to PARP inhibitors. PMID: 21577210
  18. In complex with its inhibitor, the crystal structure of PARP2 alpha-helix 5 that contains glutamate residue Glu335 is closer to the active site than in both PARP1 and PARP3 and suggests a mechanism for a weak bias toward PARP2. PMID: 20092359
  19. The PARP-2 gene might be associated with azoospermia by meiotic arrest PMID: 19806447
  20. PARP-1 and PARP-2 act as positive regulators of genomic stability in eukaryotic cells by counteracting topoisomerase I-induced DNA damage PMID: 14699148
  21. PARP-2 and PARP-1 interact with TTF-1 and regulate the expression of surfactant protein B, a protein required for lung function PMID: 16461352
  22. cells from old subjects show a constitutive expression level of both parp 1 and parp 2 genes reduced by a half PMID: 17518695
  23. Determination of Poly (ADP-ribose) polymerase (PARP) homologues in human ejaculated sperm and its correlation with sperm maturation. PMID: 18339380
  24. PARP-1-but not PARP-2-is required for proper expression of major genes involved in regulation of apoptosis PMID: 18587655
  25. Results provide strong evidence that lysine 36 of PARP-2 is a critical residue for proper nuclear targeting of PARP-2 and consequently for the execution of its biological functions. PMID: 18644123
  26. 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 PMID: 18676401

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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