Histone deacetylase 4 (HDAC4) is a member of the class IIa HDAC family, which plays a critical role in epigenetic regulation by removing acetyl groups from histone proteins, leading to chromatin condensation and transcriptional repression. HDAC4 is involved in diverse cellular processes, including differentiation, apoptosis, and stress responses. It contains a conserved C-terminal catalytic domain and an N-terminal regulatory domain that mediates interactions with transcription factors, such as MEF2. and other co-regulators. HDAC4 is highly expressed in tissues like the brain, heart, and skeletal muscle, and its activity is modulated by post-translational modifications, including phosphorylation and nucleocytoplasmic shuttling. Dysregulation of HDAC4 has been linked to cancer, neurodegenerative diseases, and cardiovascular disorders, making it a therapeutic target of interest.
HDAC4 antibodies are essential tools for studying its expression, localization, and function in both physiological and pathological contexts. These antibodies are widely used in techniques such as Western blotting, immunohistochemistry, immunofluorescence, and chromatin immunoprecipitation (ChIP). High-quality HDAC4 antibodies specifically recognize epitopes within its unique structural regions, distinguishing it from other HDAC isoforms. Researchers often validate antibody specificity using knockout cell lines or siRNA-mediated HDAC4 knockdown. Both monoclonal and polyclonal HDAC4 antibodies are available, each offering distinct advantages in sensitivity and application versatility. Understanding HDAC4's role through these antibodies contributes to advancing research in epigenetics, disease mechanisms, and targeted drug development.