The histone H2B (formylK108) antibody is a specialized tool used to detect the post-translational modification of lysine 108 (K108) on histone H2B, specifically formylation. Histones, including H2B, are core components of nucleosomes, playing critical roles in chromatin structure and epigenetic regulation. Post-translational modifications (PTMs) of histones, such as acetylation, methylation, phosphorylation, and formylation, dynamically influence DNA accessibility, gene expression, and cellular processes like DNA repair and apoptosis.
Formylation, a less-studied histone modification, involves the addition of a formyl group to lysine residues. While its precise biological role remains under investigation, formylation may compete with or mimic other lysine modifications (e.g., acetylation), potentially altering chromatin interactions or signaling pathways. The formylK108 modification on H2B has been implicated in DNA damage response and transcriptional regulation, though mechanistic insights are still emerging.
This antibody enables researchers to study the spatial and temporal dynamics of H2B formylK108 in cells or tissues via techniques like Western blotting, immunofluorescence, or chromatin immunoprecipitation (ChIP). Its specificity is validated using knockout controls or competitive peptides to ensure accurate detection. As formylation gains attention in fields like cancer biology, neurodegeneration, and epigenetics, the H2B (formylK108) antibody serves as a vital reagent for exploring the functional significance of this modification in health and disease.