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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 Dimethylation of histone 3 lysine 14 (H3K14Me2) is enriched in the promoter region of tumor suppressor candidate 3 (TUSC3), but not that of GAPDH, in DLD-1 and HCT116 cells.3 Ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1) can bind to dimethylated H3K14 and suppress acetylation of H3K14. H3K14Me2 levels increase during transdifferentiation of rat Thy-1(+) Lin(-) bone marrow cells into hepatocytes in vitro.4 Cayman’s Histone H3K14Me2 Monoclonal Antibody (RM165) can be used for ELISA, 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. UHRF1-
4. Epigenetic modifications of histone H3 during the transdifferentiation of Thy-