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Histone H2A 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 Histones are globular proteins with unstructured N-terminal tails and are subject to a variety of post-translational modifications, such as methylation, acetylation, phosphorylation, and citrullination, that can influence chromatin structure and regulate gene transcription.1,2 Phosphorylation of histone H2A at serine 1 (H2AS1Ph) is mediated by p90 ribosomal S6 kinase 5 (RSK5) and is associated with transcriptional repression.3 H2AS1Ph is enriched during mitosis in C. elegans, Drosophila, and HeLa cells, as well as during meiotic recombination in mouse spermatozoa.4,5,6 Cayman's Histone H2AS1Ph Monoclonal Antibody (RM216) can be used for ELISA, immunocytochemistry (ICC), multiplex-based assay, and Western blot (WB) applications. This antibody is cross-reactive with histone H4 phosphorylated at serine 1 (H4S1Ph).
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1. Writing, erasing and reading histone lysine methylations. Exp. Mol. Med. 49(4), e324 (2017).
2. Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation. J. Cell Biol. 184(2), 205-213 (2009).
3. Phosphorylation of histone H2A inhibits transcription on chromatin templates. The Journal of Biological Chemisty 279(21), 21866-21872 (2004).
4. The enhancement of histone H4 and H2A serine 1 phosphorylation during mitosis and S-
5. Histone post-
6. Dynamics of histone H2A, H4 and HS1ph during spermatogenesis with a focus on chromatin condensation and maturity of spermatozoa. Sci. Rep. 6, 25089 (2016).