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Histone H3 is a nuclear protein and a component of the nucleosome core, a basic unit of chromatin, that is essential for organizing genomic DNA in eukaryotic nuclei.1 It is a globular protein that contains an unstructured N-terminal tail that extends outside of the nucleosome core and is subject to various post-translational modifications (PTMs), including methylation, phosphorylation, acetylation, and citrullination.1,2 Phosphorylation of histone H3 at serine 10 (H3S10Ph) is correlated with chromatin condensation during mitosis and with transcriptional activation of genes during interphase.3,4 H3S10Ph does not inhibit binding of the ADD domain of the chromatin-remodeling protein ATRX to histone H3 N-terminal peptides due to its positioning away from the core peptide binding sequence but does decrease binding of the HP1α chromodomain (CD) when the histone H3 peptide is also trimethylated at lysine 9.5 Low median levels of H3S10Ph in tumor tissue isolated from patients with oral squamous cell carcinoma (OSCC) are associated with cervical lymph node metastasis.6 Cayman's Histone H3S10Ph Monoclonal Antibody (Clone RM163) can be used for ELISA, immunocytochemistry (ICC), multiplex-based assay, and Western blot (WB) applications.
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1. Writing, erasing and reading histone lysine methylations. Exp. Mol. Med. 49(4), e324 (2017).
2. Histone posttranslational modifications: Potential role in diagnosis, prognosis, and therapeutics of cancer. Prognostic Epigenetics 15, 351-373 (2019).
3. Histone H3 phosphorylation -
4. Phosphorylation of serine 10 in histone H3, what for? J. Cell. Sci. 116(Pt. 18), 3677-3685 (2003).
5. ATRX tolerates activity-
6. Prognostic value of histone H3 serine 10 phosphorylation and histone H4 lysine 12 acetylation in oral squamous cell carcinoma. Histopathology 74(2), 227-238 (2019).