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The protein encoded by PARP3 belongs to the PARP family. Zusätzlich bieten wir Ihnen PARP3 Proteine (6) und und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 103 products:
Cow (Bovine) Polyclonal PARP3 Primary Antibody für IHC, WB - ABIN2778113
Augustin, Spenlehauer, Dumond, Ménissier-De Murcia, Piel, Schmit, Apiou, Vonesch, Kock, Bornens, De Murcia: PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. in Journal of cell science 2003
Show all 2 Pubmed References
Polyclonal PARP3 Primary Antibody für ELISA - ABIN539677
Rouleau, McDonald, Gagné, Ouellet, Droit, Hunter, Dutertre, Prigent, Hendzel, Poirier: PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery. in Journal of cellular biochemistry 2007
Parp3 is crucial in the early stages of zebrafi (zeige ARHGEF16 Antikörper)sh development, possibly by exerting its transcriptional regulatory functions as early as during the specification of the neural plate border
These data identify PARP3 as a molecular sensor of nicked nucleosomes.
PARP3 controls of TGFbeta (zeige TGFB1 Antikörper)-induced epithelial mesenchymal transformation and acquisition of stem-like cell features by stimulation transglutaminase 2 (zeige TGM2 Antikörper)/SNAI1 (zeige SNAI1 Antikörper) signaling.
Data indicate that PARP3, a DNA damage-activated ADP-ribosyltransferase, can mono-ADP-ribosylate double-stranded DNA ends.
In a process of single-strand DNA repair, PARP3 mono-ADP-ribosylates nucleosomal histone H2B.
we found that PARP3 interacted with FoxM1 (zeige FOXM1 Antikörper) to enhance its transcriptional activity and conferred glioblastoma cell radioresistance. Thus, our data suggest that PARP3 could be a therapeutic target to overcome radioresistance in glioblastoma
Identification of ADP-ribosylation sites in PARP3 and the determination of the extent ofpoly(ADP-ribosyl)ated residues in this protein was performed.
MiR (zeige MLXIP Antikörper)-630 reduced apoptosis by downregulating several apoptotic modulators, PARP3, DDIT4 (zeige DDIT4 Antikörper), and EP300 (zeige EP300 Antikörper).
In some cancer cells, repression of PARP3 could be responsible for an increased telomerase activity.
PARP3 likely facilitates the recruitment of Ku80 (zeige XRCC5 Antikörper) to double strand breaks to antagonize DNA end resection but facilitate Ku-mediated accurate classical non-homologous end-joining.
PARP3 gene occupancy in the human neuroblastoma (zeige ARHGEF16 Antikörper) cell line SK-N-SH occurs preferentially with developmental genes regulating cell fate specification, tissue patterning, craniofacial development and neurogenesis.
We show that Poly(ADP)ribose polymerase 3 (Parp3), an enzyme recently implicated in DNA repair, contributes to antibody diversification by negatively regulating class switch recombination without affecting somatic hypermutation.
PARP-3 has a role in chromosomal DNA double-strand break repair.
We cloned and sequenced the cDNAs of the mouse PARP-3 (Adprt3) gene encoding poly(ADP-ribose) polymerase 3 and of the closely linked U3-55k (zeige RRP9 Antikörper) gene coding for the U3 small nucleolar ribonucleoprotein complex-associated 55-kilodalton protein.
The protein encoded by this gene belongs to the PARP family. These enzymes modify nuclear proteins by poly-ADP-ribosylation, which is required for DNA repair, regulation of apoptosis, and maintenance of genomic stability. This gene encodes the poly(ADP-ribosyl)transferase 3, which is preferentially localized to the daughter centriole throughout the cell cycle. Alternatively spliced transcript variants encoding different isoforms have been identified.
NAD(+) ADP-ribosyltransferase 3
, poly [ADP-ribose] polymerase 3
, poly[ADP-ribose] synthase 3
, ADP-ribosyltransferase (NAD+; poly (ADP-ribose polymerase)-like 3
, poly (ADP-ribose) polymerase family, member 3
, Poly synthetase 3
, poly [ADP-ribose] polymerase 3-like
, ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase)-like 2
, ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase)-like 3
, ADP-ribosyltransferase diphtheria toxin-like 3
, NAD+ ADP-ribosyltransferase 3
, poly(ADP-ribose) synthetase-3
, poly[ADP-ribose] synthetase 3
, A DP-ribosyltransferase (NAD+; poly (ADP-ribose polymerase)-like 3
, ADP-ribosyltransferase (NAD+, poly (ADP-ribose polymerase)-like 3
, Poly[ADP-ribose] synthetase-3
, poly (ADP-ribosyl) transferase-like 3