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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 H3K36 is catalyzed by SET domain-containing histone methyltransferases including SET2, HYPB, NSD1, and ASH1L, and mutation of these methyltransferases is associated with various diseases, including multiple myeloma and Sotos syndrome.3,4,5 H3K36Me2 is enriched at the coding regions of genes and correlates with the initiation, but not maintenance, of active transcription, heterochromatin maintenance, and DNA break repair.4,6,7 Cayman's Histone H3K36Me2 Monoclonal Antibody (RM141) can be used for ELISA, multiplex-based assays, 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. Understanding histone H3 lysine 36 methylation and its deregulation in disease. Cell Mol. Life Sci. 76(15), 2899-2916 (2019).
4. Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-
5. Identification and characterization of a novel human histone H3 lysine 36-
6. Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription. The Journal of Biological Chemisty 284(12), 7970-7976 (2009).
7. Structural and biochemical insights into MLL1 core complex assembly. Structure 19(1), 101-108 (2011).