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Human Polyclonal PARP2 Primary Antibody für 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 für 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 für 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 (zeige TP53BP1 Antikörper) at DNA damage sites, allowing efficient CtIP (zeige RBBP8 Antikörper)-dependent DNA end-resection
either PARP1 (zeige PARP1 Antikörper) or PARP2 are sufficient for near-normal XRCC1 (zeige XRCC1 Antikörper) 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 (zeige MLXIP Antikörper)-149 expression are involved in the pathogenesis of hepatocellular carcinomas (HCC (zeige FAM126A Antikörper)) and are poor prognosis factors in patients with HCC (zeige FAM126A Antikörper).
Data show that E7449 represents a dual Poly(ADP-ribose) Polymerase 1 (zeige PARP1 Antikörper)/2 and tankyrase 1 (zeige TNKS Antikörper)/2 inhibitor which has the advantage of targeting Wnt (zeige WNT2 Antikörper)/beta-catenin (zeige CTNNB1 Antikörper) signaling addicted tumors.
The initial affinity between the PARP1 (zeige PARP1 Antikörper), 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 (zeige PARP1 Antikörper) 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 (zeige PARP1 Antikörper), the other major DDR (zeige DDR1 Antikörper)-PARP (zeige COL11A2 Antikörper), and highlights the specialization of the multi-domain architectures of DDR (zeige DDR1 Antikörper)-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 (zeige PARP1 Antikörper) or -2 is likely to play a role in muscle protein catabolism via oxidative stress, NF-kappaB (zeige NFKB1 Antikörper) signaling, and enhanced proteasomal degradation in cancer-induced cachexia.
PARP1 (zeige PARP1 Antikörper)/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 (zeige PARP1 Antikörper) and PARP2 at H2AX (zeige H2AFX Antikörper)-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 (zeige PARP1 Antikörper) in nonhomologous end-joining-deficient cells.
Data show reduced tumor burden through increased oxidative stress in lung adenocarcinoma cells of PARP-1 (zeige PARP1 Antikörper) and PARP-2 knockout mice.
PARP-2 has an essential role in erythropoiesis by limiting replicative stress in erythroid progenitors.
PARP-1 (zeige PARP1 Antikörper) and -2 play a role in cancer-induced cachexia, thus selective pharmacological inhibition of PARP-1 (zeige PARP1 Antikörper) and -2 may be of interest in clinical settings
the depletion of PARP-2 leads to lower HDL (zeige HSD11B1 Antikörper) 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 (zeige XRCC5 Antikörper) and ku80 (zeige XRCC5 Antikörper) parp1 parp2 mutants, corroborating with a role of KU in preventing DSB end resection. Deletion lengths did not significantly differ between ku80 (zeige XRCC5 Antikörper) and ku80 (zeige XRCC5 Antikörper) parp1 parp2 mutants, suggesting that a KU- and PARP (zeige PARP1 Antikörper)-independent b-NHEJ mechanism becomes active in these mutants.
whilst all isoforms of PARP (zeige PARP1 Antikörper) were localized to the nucleus they are also present in non-nuclear locations with parp1 and parp3 (zeige PARP3 Antikörper) 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 (zeige ROS1 Antikörper)).
PARP (zeige PARP1 Antikörper) isoforms play a minor role in telomere length maintenance in Arabidopsis.
Evidence suggests a link between the glutathione pool and PARP (zeige PARP1 Antikörper) 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