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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 H3 at lysine 4 (H3K4Me2) is found at active and primed, but inactive, loci.3,4 It is enriched in gene promoter regions and overlaps with transcription factor binding sites. Low tumor levels of H3K4Me2 positively correlate with decreased overall and disease-free survival in pancreatic cancer patients.5 Cayman's Histone H3K4Me2 Monoclonal Antibody (RM135) can be used for chromatin immunoprecipitation (ChIP), 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 Lys 4 methylation: Caught in a bind? Genes Dev. 20(20), 2779-2786 (2006).
4. H3K4me2 reliably defines transcription factor binding regions in different cells. Genomics 103(2-3), 222-228 (2014).
5. The cellular level of histone H3 lysine 4 dimethylation correlates with response to adjuvant gemcitabine in Japanese pancreatic cancer patients treated with surgery. Eur. J. Surg. Oncol. 38(11), 1051-1057 (2012).