KDM5B (lysine-specific demethylase 5B), also known as JARID1B or PLU-1. is a member of the KDM5 family of histone demethylases that specifically catalyze the removal of methyl groups from di- and tri-methylated lysine 4 on histone H3 (H3K4me2/me3), a chromatin mark associated with active transcription. By modulating H3K4 methylation states, KDM5B plays a critical role in regulating gene expression, cellular differentiation, and epigenetic memory. It contains conserved structural domains, including the JmjC domain responsible for its enzymatic activity.
Dysregulation of KDM5B is linked to cancer progression, stem cell maintenance, and drug resistance. Overexpression of KDM5B has been observed in various cancers (e.g., breast cancer, melanoma, lung cancer), where it suppresses tumor suppressor genes and promotes oncogenic pathways. This enzyme is also implicated in maintaining cancer stem cell populations, contributing to tumor recurrence and therapy resistance.
KDM5B antibodies are essential tools in research for detecting protein expression, localization, and interaction partners via techniques like Western blotting, immunofluorescence, or chromatin immunoprecipitation (ChIP). They enable studies exploring KDM5B's role in epigenetic regulation, cancer biology, and response to therapeutic inhibitors targeting its demethylase activity. Validated antibodies are critical for ensuring specificity, given the high homology among KDM5 family members. Research on KDM5B continues to advance understanding of epigenetic mechanisms and potential therapeutic strategies in oncology.