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Mouse Anti-PARP3 Recombinant Antibody (B-7) (CBMAB-P0822-YC)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
B-7
Antibody Isotype
IgG
Application
WB, IP, IF, ELISA

Basic Information

Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
poly (ADP-ribose) polymerase family, member 3
Introduction
PARP3 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.
Entrez Gene ID
Human10039
Mouse235587
Rat300985
UniProt ID
HumanQ9Y6F1
MouseQ3ULW8
RatQ5U2U3
Alternative Names
Poly(ADP-Ribose) Polymerase Family Member 3; ADP-Ribosyltransferase (NAD+; Poly (ADP-Ribose) Polymerase)-Like 3; ADP-Ribosyltransferase Diphtheria Toxin-Like 3; NAD(+) ADP-Ribosyltransferase 3; Poly(ADP-Ribose) Synthetase-3; NAD+ ADP-Ribosyltransferase 3; Poly[ADP-Ribose] Synthase 3; PADPRT-3; ADPRTL3; ADPRT-3; ADPRT3;
Function
Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:16924674, PubMed:20064938, PubMed:21211721, PubMed:21270334, PubMed:25043379, PubMed:24598253).
Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (PubMed:20064938, PubMed:25043379).
In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:25043379).
Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334).
Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (PubMed:21211721).
Cooperates with the XRCC5-XRCC6 (Ku80-Ku70) heterodimer to limit end-resection thereby promoting accurate NHEJ (PubMed:24598253).
Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as XRCC5 and XRCC6 (PubMed:16924674, PubMed:24598253).
ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334).
May link the DNA damage surveillance network to the mitotic fidelity checkpoint (PubMed:16924674).
In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks (PubMed:29361132, PubMed:29520010).
Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin (By similarity).
Biological Process
DNA ADP-ribosylationManual Assertion Based On ExperimentIDA:UniProtKB
DNA repairManual Assertion Based On ExperimentTAS:ProtInc
Double-strand break repairManual Assertion Based On ExperimentIDA:MGI
Negative regulation of isotype switchingISS:UniProtKB
Negative regulation of telomerase RNA reverse transcriptase activityManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of DNA ligationManual Assertion Based On ExperimentIGI:MGI
Positive regulation of double-strand break repair via nonhomologous end joiningManual Assertion Based On ExperimentIDA:UniProtKB
Protein ADP-ribosylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein auto-ADP-ribosylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein localization to site of double-strand breakManual Assertion Based On ExperimentIMP:MGI
Protein mono-ADP-ribosylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein poly-ADP-ribosylationManual Assertion Based On ExperimentIBA:GO_Central
Regulation of mitotic spindle organizationManual Assertion Based On ExperimentIMP:MGI
Telomere maintenanceManual Assertion Based On ExperimentIMP:MGI
Cellular Location
Nucleus
Chromosome
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole
Almost exclusively localized in the nucleus and appears in numerous small foci and a small number of larger foci whereas a centrosomal location has not been detected (PubMed:16924674).
In response to DNA damage, localizes to sites of double-strand break (PubMed:21270334).
Preferentially localized to the daughter centriole (PubMed:10329013).
PTM
Auto-mono-ADP-ribosylated.
More Infomation

Nguekeu-Zebaze, L., Hanini, N., Noll, A., Wadier, N., Amé, J. C., Roegel, L., & Dantzer, F. (2022). PARP3 supervises G9a-mediated repression of adhesion and hypoxia-responsive genes in glioblastoma cells. Scientific Reports, 12(1), 15534.

van Beek, L., McClay, É., Patel, S., Schimpl, M., Spagnolo, L., & Maia de Oliveira, T. (2021). PARP power: a structural perspective on PARP1, PARP2, and PARP3 in DNA damage repair and nucleosome remodelling. International journal of molecular sciences, 22(10), 5112.

Rodriguez-Vargas, J. M., Martin-Hernandez, K., Wang, W., Kunath, N., Suganthan, R., Amé, J. C., ... & Dantzer, F. (2020). Parp3 promotes astrocytic differentiation through a tight regulation of Nox4-induced ROS and mTorc2 activation. Cell Death & Disease, 11(11), 954.

Kutuzov, M. M., Belousova, E. A., Ilina, E. S., & Lavrik, O. I. (2020). Impact of PARP1, PARP2 & PARP3 on the base excision repair of nucleosomal DNA. Mechanisms of Genome Protection and Repair, 47-57.

Gil-Kulik, P., Dudzińska, E., Radzikowska-Büchner, E., Wawer, J., Jojczuk, M., Nogalski, A., ... & Kocki, J. (2020). Different regulation of PARP1, PARP2, PARP3 and TRPM2 genes expression in acute myeloid leukemia cells. BMC cancer, 20, 1-9.

Centko, R. M., Carlile, G. W., Barne, I., Patrick, B. O., Blagojevic, P., Thomas, D. Y., & Andersen, R. J. (2020). Combination of selective PARP3 and PARP16 inhibitory analogues of latonduine a corrects F508del-CFTR Trafficking. ACS omega, 5(40), 25593-25604.

Gu, Z., Pan, W., Chen, W., Lian, Q., Wu, Q., Lv, Z., ... & Ge, X. (2019). New perspectives on the plant PARP family: Arabidopsis PARP3 is inactive, and PARP1 exhibits predominant poly (ADP-ribose) polymerase activity in response to DNA damage. BMC plant biology, 19, 1-18.

Rodriguez-Vargas, J. M., Nguekeu-Zebaze, L., & Dantzer, F. (2019). PARP3 comes to light as a prime target in cancer therapy. Cell Cycle, 18(12), 1295-1301.

Beck, C., Rodriguez-Vargas, J. M., Boehler, C., Robert, I., Heyer, V., Hanini, N., ... & Dantzer, F. (2019). PARP3, a new therapeutic target to alter Rictor/mTORC2 signaling and tumor progression in BRCA1-associated cancers. Cell Death & Differentiation, 26(9), 1615-1630.

Sherstyuk, Y. V., Ivanisenko, N. V., Zakharenko, A. L., Sukhanova, M. V., Peshkov, R. Y., Eltsov, I. V., ... & Abramova, T. V. (2019). Design, synthesis and molecular modeling study of conjugates of ADP and morpholino nucleosides as a novel class of inhibitors of PARP-1, PARP-2 and PARP-3. International Journal of Molecular Sciences, 21(1), 214.

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For research use only. Not intended for any clinical use.

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