Parp2 Antibody

Code CSB-PA017466XA01MO
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Product Details

Full Product Name
Rabbit anti-Mus musculus (Mouse) Parp2 Polyclonal antibody
Uniprot No.
Target Names
Parp2
Alternative Names
Parp2 antibody; Adprt2 antibody; Adprtl2 antibody; Aspartl2 antibody; Poly [ADP-ribose] polymerase 2 antibody; PARP-2 antibody; mPARP-2 antibody; EC 2.4.2.30 antibody; ADP-ribosyltransferase diphtheria toxin-like 2 antibody; ARTD2 antibody; DNA ADP-ribosyltransferase PARP2 antibody; EC 2.4.2.- antibody; NAD(+) ADP-ribosyltransferase 2 antibody; ADPRT-2 antibody; Poly[ADP-ribose] synthase 2 antibody; pADPRT-2 antibody; Protein poly-ADP-ribosyltransferase PARP2 antibody; EC 2.4.2.- antibody
Raised in
Rabbit
Species Reactivity
Mus musculus (Mouse)
Immunogen
Recombinant Mus musculus (Mouse) Parp2 protein
Immunogen Species
Mus musculus (Mouse)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB (ensure identification of antigen)
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (14-16 weeks)

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Target Background

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.
Gene References into Functions
  1. PARP2 is preferentially activated by poly(ADP-ribose) (PAR) and subsequently catalyzes branched PAR chain synthesis. PMID: 30104678
  2. Peripheral T-cell number was not affected in single PARP-2-deficient mice. Double-deficiency in PARP-1/PARP-2 in T-cells led to highly aggressive T-cell lymphomas. PMID: 28181505
  3. PARP2 protein deficiency protected mice from Concanavalin A -induced Liver Damage. PMID: 28751426
  4. Activation of either PARP-1 or -2 is likely to play a role in muscle protein catabolism via oxidative stress, NF-kappaB signaling, and enhanced proteasomal degradation in cancer-induced cachexia. PMID: 28177129
  5. PARP1/2 inhibitor simmiparib causes growth inhibition in cancer cell- or tissue-derived xenografts in nude mice. PMID: 27847302
  6. The findings highlight specific non-overlapping functions of PARP1 and PARP2 at H2AX-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 in nonhomologous end-joining-deficient cells. PMID: 27373144
  7. Data show reduced tumor burden through increased oxidative stress in lung adenocarcinoma cells of PARP-1 and PARP-2 knockout mice. PMID: 26700152
  8. PARP-2 has an essential role in erythropoiesis by limiting replicative stress in erythroid progenitors. PMID: 25501596
  9. PARP-1 and -2 play a role in cancer-induced cachexia, thus selective pharmacological inhibition of PARP-1 and -2 may be of interest in clinical settings PMID: 26432600
  10. the depletion of PARP-2 leads to lower HDL levels which represent a risk factor to cardiovascular diseases. PMID: 24365238
  11. This study represents the first description of a significant role for PARP-2 in neuroinflammation and neurological dysfunction in Experimental autoimmune encephalomyelitis PMID: 23607899
  12. our data show that PARP-2 can directly regulate base excision repair proteins PMID: 23357680
  13. Our results show that Parp-2 plays essential roles in the surveillance of genome integrity of stem cell hematopoiesis by orchestrating DNA repair and restraining p53-induced and Puma-mediated apoptosis. PMID: 23678004
  14. PARP2 activity mobilizes intracellular TRPM2 channels in a Parp1-/- background. PMID: 22751932
  15. Identify PARP-2 as a mediator of doxorubicin toxicity by regulating vascular SIRT1 activity and mitochondrial biogenesis. PMID: 21921080
  16. Inhibition of PARP1 and PARP2 (by genetic or pharmacological means) leads to increased TOP2B activity in elongating spermatids. PMID: 21228215
  17. PARP-2 deletion in mice increases SIRT1 levels, promotes energy expenditure, and increases mitochondrial content. PMID: 21459329
  18. role of PARP-2 activity in the maintenance of telomere integrity; PARP-2 physically binds to TRF2 with high affinity PMID: 14749375
  19. crystal structure of the catalytic fragment of murine PARP-2, at 2.8 A resolution PMID: 14739238
  20. We conclude that PARP-2 contributes substantially to nuclear translocation of AIF and infarct size after transient focal cerebral ischemia in male mice, but that protection is disproportionate to the attenuation of overall PARP activity. PMID: 20236222
  21. a synergistic interaction between Parp-2 and p53 in tumour suppression through the role of Parp-2 in DNA-damage response and genome integrity surveillance PMID: 20154718
  22. Caspase-8 not only triggers and amplifies the apoptotic process at cytoplasmic sites but can also act as an executioner at nuclear levels where it cleaves PARP-2 PMID: 12065591
  23. functional interaction with poly ADP ribose pomymerase 1 and role of that interaction in chromosome stability and embryo development PMID: 12727891
  24. genetic interactions between PARP-1, PARP-2, Atm play an essential role during early embryogenesis [review] PMID: 15279798
  25. role for PARP-2 as an important mediator of T-cell survival during thymopoiesis by preventing the activation of DNA damage-dependent apoptotic response during the multiple rounds of TCRalpha rearrangements preceding a positively selected TCR PMID: 16946705
  26. These findings indicate that, in addition to its well known role in DNA repair, Parp-2 exerts essential functions during meiosis I and haploid gamete differentiation. PMID: 17001008
  27. PPAR-2 controls adipocyte differentiation and adipose tissue function through the regulation of the activity of the retinoid X receptor/PPARgamma heterodimer PMID: 17951580
  28. These results provide evidence that acetylation of PARP-2 is a key post-translational modification that may regulate DNA binding and consequently also the enzymatic activity of PARP-2. PMID: 18436469
  29. Selective PARP-2 inhibitors increase apoptosis in hippocampal slices but protect cortical cells in models of post-ischaemic brain damage. PMID: 19422384
  30. Data show that Parp2 interacts significantly with both the transition protein TP2 and the transition chaperone HSPA2, whereas Parp1 binds weakly to HSPA2. PMID: 19607827

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Subcellular Location
Nucleus. Chromosome.
Tissue Specificity
Widely expressed; the highest levels were in testis followed by ovary. Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult.
Database Links
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