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The protein encoded by PARP3 belongs to the PARP family. Additionally we are shipping PARP3 Proteins (6) and many more products for this protein.
Showing 10 out of 90 products:
Cow (Bovine) Polyclonal PARP3 Primary Antibody for 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 references for ABIN2778113
Human Polyclonal PARP3 Primary Antibody for WB - ABIN390264
Urbánek, Paces, Králová, Dvorák, Paces: Cloning and expression of PARP-3 (Adprt3) and U3-55k, two genes closely linked on mouse chromosome 9. in Folia biologica 2002
Human Polyclonal PARP3 Primary Antibody for ELISA, WB - ABIN308468
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
Human Polyclonal PARP3 Primary Antibody for IHC, ELISA - ABIN1534478
Johansson: A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues. in Genomics 1999
Parp3 is crucial in the early stages of zebrafi (show ARHGEF16 Antibodies)sh development, possibly by exerting its transcriptional regulatory functions as early as during the specification of the neural plate border
we found that PARP3 interacted with FoxM1 (show FOXM1 Antibodies) 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 (show MLXIP Antibodies)-630 reduced apoptosis by downregulating several apoptotic modulators, PARP3, DDIT4 (show DDIT4 Antibodies), and EP300 (show EP300 Antibodies).
In some cancer cells, repression of PARP3 could be responsible for an increased telomerase activity.
PARP3 likely facilitates the recruitment of Ku80 (show XRCC5 Antibodies) 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 (show ARHGEF16 Antibodies) cell line SK-N-SH occurs preferentially with developmental genes regulating cell fate specification, tissue patterning, craniofacial development and neurogenesis.
PARP3 is a critical player in the stabilization of the mitotic spindle and in telomere integrity by associating and regulating the mitotic components NuMA (show NUMA1 Antibodies) and tankyrase 1 (show TNKS Antibodies).
PARP-3 has a role in chromosomal DNA double-strand break repair.
the interaction between PARP-1 (show PARP1 Antibodies) and PARP-3 is unrelated to DNA single-strand break repair
PARP-3 is a nuclear protein involved in transcriptional silencing and in the cellular response to DNA damage
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.
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 (show RRP9 Antibodies) 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