anti-Poly (ADP-Ribose) Polymerase Family, Member 10 (PARP10) Antibodies

Human Poly (ADP-Ribose) Polymerase Family, Member 10 (PARP10) interaction partners

1. PARP10 promotes cellular proliferation, and its overexpression alleviates cellular sensitivity to replication stress and fosters the restart of stalled replication forks. In mouse xenograft studies, PARP10 loss reduces the tumorigenesis activity of HeLa cells. Its overexpression results in tumor formation by non-transformed RPE-1 cells. PARP10 may promote cellular transformation by alleviating replication stress.

2. Study shows that PARP10 is downregulated in intrahepatic metastatic hepatocellular carcinoma. Further results provide evidence that deficiency of PARP10 markedly increased the migration and invasion of tumor cells through regulation of epithelial-mesenchymal transition, and that PARP10 expression inhibited tumor metastasis in vivo.

3. PARP10 expression decreased upon fasting, a condition that is characterized by increases in mitochondrial biogenesis. Finally, lower PARP10 expression is associated with increased fatty acid oxidation

4. ARTD10 plays roles in immunity, metabolism ,apoptosis and DNA damage repair. [review]

5. PARP10 binding to PCNA is required for translesion DNA synthesis.

6. study results show that the interaction between PARP10 and NS1 of H5N1 avian influenza virus can change cell cycle, and PARP10 can affect virus replication

7. novel PARP enzyme involved in the control of cell proliferation

8. Overexpression of PARP10 results in loss of cell viability, although down-expression by short hairpin RNA leads to delayed G1 progression and concomitant cell death.

9. alternative catalytic mechanism for PARP10 compared to PARP1 in which the acidic target residue of the substrate functionally substitutes for the catalytic glutamate by using substrate-assisted catalysis to transfer ADP-ribose

Mouse (Murine) Poly (ADP-Ribose) Polymerase Family, Member 10 (PARP10) interaction partners

1. murine Artd8 macrodomain constructs can serve as a tool to evaluate intracellular ARTD10 auto-modification levels using the described methods, while the human ARTD8 macrodomains are less suited because of ADPr-independent binding to ARTD10. Protocols for co-immunoprecipitation and co-localization experiments are described in detail.