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Human Polyclonal PARP2 Primary Antibody for WB - ABIN151360
Ovadje, Ammar, Guerrero, Arnason, Pandey: Dandelion root extract affects colorectal cancer proliferation and survival through the activation of multiple death signalling pathways. in Oncotarget 2016
Human Polyclonal PARP2 Primary Antibody for ELISA, WB - ABIN250990
Kofler, Otsuka, Zhang, Noppens, Grafe, Koh, Dawson, de Murcia, Hurn, Traystman: Differential effect of PARP-2 deletion on brain injury after focal and global cerebral ischemia. in Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 2005
Human Polyclonal PARP2 Primary Antibody for ChIP, IP - ABIN2668807
Hanzlikova, Gittens, Krejcikova, Zeng, Caldecott: Overlapping roles for PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin. in Nucleic acids research 2016
PARP2 specifically limits the accumulation of the resection barrier factor 53BP1 (show TP53BP1 Antibodies) at DNA damage sites, allowing efficient CtIP (show RBBP8 Antibodies)-dependent DNA end-resection
either PARP1 (show PARP1 Antibodies) or PARP2 are sufficient for near-normal XRCC1 (show XRCC1 Antibodies) recruitment at oxidative single-strand breaks
Studies indicate that poly(ADP-ribose) polymerase 2 (PARP2) is involved in the differentiation of several cell types, including erythrocytes, T cells and adipocytes.
Findings indicate that Increased poly(ADP-ribose) polymerase-2 (PARP-2) expression and loss of micrRNA miR (show MLXIP Antibodies)-149 expression are involved in the pathogenesis of hepatocellular carcinomas (HCC (show FAM126A Antibodies)) and are poor prognosis factors in patients with HCC (show FAM126A Antibodies).
Data show that E7449 represents a dual Poly(ADP-ribose) Polymerase 1 (show PARP1 Antibodies)/2 and tankyrase 1 (show TNKS Antibodies)/2 inhibitor which has the advantage of targeting Wnt (show WNT2 Antibodies)/beta-catenin (show CTNNB1 Antibodies) signaling addicted tumors.
The initial affinity between the PARP1 (show PARP1 Antibodies), 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 (show PARP1 Antibodies) and PARP2 on DNA damages.
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
Our study differentiates the functions of PARP-2 domains from those of PARP-1 (show PARP1 Antibodies), the other major DDR (show DDR1 Antibodies)-PARP (show COL11A2 Antibodies), and highlights the specialization of the multi-domain architectures of DDR (show DDR1 Antibodies)-PARPs.
Interaction of PARP-2 with AP site containing DNA
Identification of ADP-ribosylation sites in PARP2 and the determination of the extent ofpoly(ADP-ribosyl)ated residues in this protein was performed.
PARP2 protein deficiency protected mice from Concanavalin A -induced Liver Damage.
Activation of either PARP-1 (show PARP1 Antibodies) or -2 is likely to play a role in muscle protein catabolism via oxidative stress, NF-kappaB (show NFKB1 Antibodies) signaling, and enhanced proteasomal degradation in cancer-induced cachexia.
PARP1 (show PARP1 Antibodies)/2 inhibitor simmiparib causes growth inhibition in cancer cell- or tissue-derived xenografts in nude mice.
The findings highlight specific non-overlapping functions of PARP1 (show PARP1 Antibodies) and PARP2 at H2AX (show H2AFX Antibodies)-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 (show PARP1 Antibodies) in nonhomologous end-joining-deficient cells.
Data show reduced tumor burden through increased oxidative stress in lung adenocarcinoma cells of PARP-1 (show PARP1 Antibodies) and PARP-2 knockout mice.
PARP-2 has an essential role in erythropoiesis by limiting replicative stress in erythroid progenitors.
PARP-1 (show PARP1 Antibodies) and -2 play a role in cancer-induced cachexia, thus selective pharmacological inhibition of PARP-1 (show PARP1 Antibodies) and -2 may be of interest in clinical settings
the depletion of PARP-2 leads to lower HDL (show HSD11B1 Antibodies) levels which represent a risk factor to cardiovascular diseases.
This study represents the first description of a significant role for PARP-2 in neuroinflammation and neurological dysfunction in Experimental autoimmune encephalomyelitis
our data show that PARP-2 can directly regulate base excision repair proteins
We found that larger deletions of >20 bp predominated after DSB repair in ku80 (show XRCC5 Antibodies) and ku80 (show XRCC5 Antibodies) parp1 parp2 mutants, corroborating with a role of KU in preventing DSB end resection. Deletion lengths did not significantly differ between ku80 (show XRCC5 Antibodies) and ku80 (show XRCC5 Antibodies) parp1 parp2 mutants, suggesting that a KU- and PARP (show PARP1 Antibodies)-independent b-NHEJ mechanism becomes active in these mutants.
whilst all isoforms of PARP (show PARP1 Antibodies) were localized to the nucleus they are also present in non-nuclear locations with parp1 and parp3 (show PARP3 Antibodies) also localised in the cytosol, and parp2 also present in the mitochondria
Studies indicate that a massive and rapid accumulation of a massive and rapid accumulation poly(ADP-ribose) polymerases AtPARP1 and AtPARP2 transcripts was observed upon treatment with ionizing radiation and reactive oxigen species (ROS (show ROS1 Antibodies)).
PARP (show PARP1 Antibodies) isoforms play a minor role in telomere length maintenance in Arabidopsis.
Evidence suggests a link between the glutathione pool and PARP (show PARP1 Antibodies) expression and activity that is perhaps related to the distribution of intracellular glutathione between the cytoplasm and the nucleus. [PARP1]
in PARP2-deficient Arabidopsis plants, the observed abiotic stress resistance can also be explained by alterations in abscisic acid levels that facilitate the induction of a wide set of defense-related genes
This gene encodes poly(ADP-ribosyl)transferase-like 2 protein, which contains a catalytic domain and is capable of catalyzing a poly(ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. The basic residues within the N-terminal region of this protein may bear potential DNA-binding properties, and may be involved in the nuclear and/or nucleolar targeting of the protein. Two alternatively spliced transcript variants encoding distinct isoforms have been found.
poly (ADP-ribose) polymerase family, member 2
, ADP-ribosyltransferase (NAD+; poly(ADP-ribose) polymerase)-like 2
, ADP-ribosyltransferase (NAD+, poly(ADP-ribose) polymerase)-like 2
, poly [ADP-ribose] polymerase 2
, poly (ADP-ribose) polymerase 2
, poly [ADP-ribose] polymerase 2-like
, ADP-ribosyltransferase diphtheria toxin-like 2
, NAD(+) ADP-ribosyltransferase 2
, poly (ADP-ribosyl) transferase-like 2
, poly(ADP-ribose) synthetase
, poly[ADP-ribose] synthase 2
, poly[ADP-ribose] synthetase 2
, ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase) 2