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Rat Anti-PARP10 Recombinant Antibody (5H11) (CBMAB-P0812-YC)


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Summary

Host Animal
Rat
Specificity
Human
Clone
5H11
Antibody Isotype
IgG1
Application
ICC, IF, IP, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
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!]

Format
10% FCS, 0.05% sodium azide
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 1-907

Target

Full Name
Poly(ADP-Ribose) Polymerase Family Member 10
Introduction
Poly(ADP-ribose) polymerases (PARPs), such as PARP10, regulate gene transcription by altering chromatin organization by adding ADP-ribose to histones. PARPs can also function as transcriptional cofactors.
Entrez Gene ID
84875
UniProt ID
Q53GL7
Alternative Names
Poly(ADP-Ribose) Polymerase Family Member 10; ADP-Ribosyltransferase Diphtheria Toxin-Like 10; ARTD10; Poly [ADP-Ribose] Polymerase 10; EC 2.4.2.30; PARP-10;
Function
ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate and aspartate residues on target proteins (PubMed:18851833, PubMed:23332125, PubMed:23474714, PubMed:25043379).
In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:18851833).
Catalyzes mono-ADP-ribosylation of GSK3B, leading to negatively regulate GSK3B kinase activity (PubMed:23332125).
Involved in translesion DNA synthesis in response to DNA damage via its interaction with PCNA (PubMed:24695737).
Biological Process
NAD biosynthesis via nicotinamide riboside salvage pathwayTAS:Reactome
Negative regulation of fibroblast proliferationManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of gene expressionManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of NF-kappaB transcription factor activityManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of protein K63-linked ubiquitinationManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of viral genome replicationManual Assertion Based On ExperimentIMP:UniProtKB
Protein ADP-ribosylationManual Assertion Based On ExperimentIMP:UniProtKB
Protein auto-ADP-ribosylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein mono-ADP-ribosylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein poly-ADP-ribosylationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of chromatin assemblyManual Assertion Based On ExperimentIDA:UniProtKB
Translesion synthesisManual Assertion Based On ExperimentIDA:UniProtKB
Viral protein processingTAS:Reactome
Cellular Location
Nucleus, nucleolus
Cytoplasm
Shuttles between the nuclear and cytoplasmic compartment (PubMed:15674325).
A subpopulation concentrates in the nucleolus during late G1/S phase (PubMed:15674325).
PTM
Stimulated through its phosphorylation by CDK2 (PubMed:16455663).
Acquires CDK-dependent phosphorylation through late-G1 to S phase, and from prometaphase to cytokinesis in the nucleolar organizing regions (PubMed:16455663).
Phosphorylation is suppressed in growth-arrested cells (PubMed:16455663).
Auto-mono-ADP-ribosylated on glutamate and lysine residues.
More Infomation

Dhoonmoon, A., & Nicolae, C. M. (2023). Mono-ADP-ribosylation by PARP10 and PARP14 in genome stability. NAR cancer, 5(1), zcad009.

Krieg, S., Pott, F., Potthoff, L., Verheirstraeten, M., Bütepage, M., Golzmann, A., ... & Korn, P. (2023). Mono-ADP-ribosylation by PARP10 inhibits Chikungunya virus nsP2 proteolytic activity and viral replication. Cellular and Molecular Life Sciences, 80(3), 72.

Di Paola, S., Matarese, M., Barretta, M. L., Dathan, N., Colanzi, A., Corda, D., & Grimaldi, G. (2022). PARP10 mediates mono-ADP-ribosylation of aurora-a regulating G2/M transition of the cell cycle. Cancers, 14(21), 5210.

Nizi, M. G., Maksimainen, M. M., Murthy, S., Massari, S., Alaviuhkola, J., Lippok, B. E., ... & Tabarrini, O. (2022). Potent 2, 3-dihydrophthalazine-1, 4-dione derivatives as dual inhibitors for mono-ADP-ribosyltransferases PARP10 and PARP15. European Journal of Medicinal Chemistry, 237, 114362.

Korn, P., Classen, A., Murthy, S., Guareschi, R., Maksimainen, M. M., Lippok, B. E., ... & Lüscher, B. (2021). Evaluation of 3‐and 4‐Phenoxybenzamides as Selective Inhibitors of the Mono‐ADP‐Ribosyltransferase PARP10. ChemistryOpen, 10(10), 939-948.

García-Saura, A. G., & Schüler, H. (2021). PARP10 multi-site auto-and histone MARylation visualized by acid-urea gel electrophoresis. Cells, 10(3), 654.

Zhao, Y., Liang, X., Wei, L., Liu, Y., Liu, J., Feng, H., ... & Wu, J. (2021). RNF114 suppresses metastasis through regulation of PARP10 in cervical cancer cells. Cancer Communications, 41(2), 187.

Tian, L., Yao, K., Liu, K., Han, B., Dong, H., Zhao, W., ... & Lu, S. (2020). PLK1/NF-κB feedforward circuit antagonizes the mono-ADP-ribosyltransferase activity of PARP10 and facilitates HCC progression. Oncogene, 39(15), 3145-3162.

Gao, X. Q., Zhang, Y. H., Liu, F., Ponnusamy, M., Zhao, X. M., Zhou, L. Y., ... & Wang, K. (2020). The piRNA CHAPIR regulates cardiac hypertrophy by controlling METTL3-dependent N 6-methyladenosine methylation of Parp10 mRNA. Nature cell biology, 22(11), 1319-1331.

Wu, C., Xiao, M., Wang, Y., Threadgill, M. D., Li, M., Tang, Y., ... & Li, X. (2020). PARP10 influences the proliferation of colorectal carcinoma cells, a preliminary study. Molecular Biology, 54, 220-228.

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

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