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Histone H2B 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 a histone fold domain with a C-terminal α-helix that facilitates nucleosome interactions and chromatin compaction, as well as an unstructured N-terminal tail that extends outside of the nucleosome core, both of which are subject to various post-translational modifications (PTMs), including ubiquitination, acetylation, methylation, and phosphorylation.1,2,3 Phosphorylation of histone H2B at serine 14 (H2BS14Ph) is associated with DNA damage and induces apoptotic chromatin condensation.4,5 H2BS14Ph also correlates with class switch recombination and somatic hypermutation in germinal center B cells.6 Cayman’s H2BS14Ph Monoclonal Antibody (Clone RM238) 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. The role of histone H2A and H2B post-
3. The C-
4. Involvement of histone PTMs in DNA repair processes in relation to age-
5. Histone H2B deacetylation at lysine 11 is required for yeast apoptosis induced by phosphorylation of H2B at serine 10. Mol. Cell 24(2), 211-220 (2006).
6. Histone modifications associated with somatic hypermutation. Immunity 23(1), 101-110 (2005).