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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWHistone H4 is one of four core histone proteins that are involved in the organization of DNA into chromatin.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 Acetylation of histone H4 at lysine 12 (H4K12Ac) is associated with chromatin relaxation and gene transcription.3 Levels of H4K12Ac are elevated in two transgenic mouse models of Alzheimer's disease, as well as in monocytes isolated from patients with mild cognitive impairment and Alzheimer's disease. H4K12Ac levels are also increased in response to chronic alcohol exposure and positively correlate with the release of the pro-inflammatory cytokine chemokine (C-C motif) ligand 8 (CCL8) in monocyte-derived dendritic cells.4 Cayman's H4K12Ac Monoclonal Antibody (RM202) can be used for chromatin immunoprecipitation (ChIP), ELISA, immunocytochemistry (ICC), multiplex-based assay, and Western blot (WB) applications.
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1. Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation. J. Cell Biol. 184(2), 205-213 (2009).
2. Writing, erasing and reading histone lysine methylations. Exp. Mol. Med. 49(4), e324 (2017).
3. Increased acetylation of histone H4 at lysine 12 (H4K12) in monocytes of transgenic Alzheimer’s mice and in human patients. Curr. Alzheimer Res. 12(8), 752-760 (2015).
4. Novel detection of post-