Acetyl-Histone H2B (Lys15) Antibody is a polyclonal antibody that specifically recognizes histone H2B when acetylated at lysine residue 15 (K15). Histone H2B is a core component of nucleosomes, which organize DNA into chromatin. Acetylation at K15 alters chromatin structure, influencing gene accessibility and transcriptional activity . This modification is classified as a candidate "onco-modification" due to its association with non-apoptotic cellular states .
K15 acetylation reduces the positive charge of histones, weakening DNA-histone interactions and promoting chromatin relaxation. This facilitates transcriptional activation .
The modification is implicated in regulating genes involved in cell proliferation and survival .
Cancer Research: K15 acetylation is observed in non-dying cells, suggesting a role in avoiding apoptosis. This makes it a potential biomarker for cancer progression .
Drug Development: Antibodies targeting this site enable the study of epigenetic therapies aimed at modulating acetylation states .
The antibody is validated for multiple techniques:
Western Blot: Detects acetylated H2B in protein extracts (e.g., HeLa cells) .
Immunohistochemistry: Visualizes acetylation patterns in tissue sections .
Chromatin Studies: Used in IP and ChIP to map acetylation sites genome-wide .