| Message: | The phosphorylation of histone H3 at serine 10 is conserved through eukaryotes, and an increase in phosphorylation has been shown to correlate with gene activation and cell growth. In vitro studies have shown that phosphorylation of histone H3 at Ser10 is coupled to acetylation at the nearby Lysine-14 residue. Histone H3 phosphorylation at Ser10 is also negatively impacted by histone methylation at lysine 9. It was observed that histone H3 phosphorylation at Ser10 is regulated by the cell cycle and has been used as mitotic marker. H3 phosphorylation (Ser10) is critical for neoplastic cell transformation. Several protein kinases, including aurora B, PPI, and PKC, are responsible for histone H3 phosphorylation at Ser10. Inhibition or activation of these protein kinases can cause the change in intracellular histone H3 phosphorylation at Ser10. Detection in the change of histone H3 phosphorylation at Ser10 associated with cell cycle, apoptosis, and inhibitor or activator treatment, would provide useful information for better understanding the pathological process of some diseases and for protein kinase-targeted drug development.
https://www.creativebiomart.net/histone-h3-phosphorylation-ser10-colorimetric-assay-kit-463109.htm |
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