HDAC3 Antibody (YA392),MedChemexpress,HY-P80152

HDAC3 Protein, a histone deacetylase with diverse substrate specificity, catalyzes the deacetylation of lysine residues situated on the N-terminal region of core histones (H2A, H2B, H3, and H4), along with various non-histone substrates. This enzymatic activity imparts an epigenetic repression tag and plays crucial roles in transcriptional regulation, cell cycle progression, and developmental events. Operating within large multiprotein complexes, HDAC3 participates in BCL6 transcriptional repressor activity by deacetylating H3 'Lys-27' (H3K27) on enhancer elements, counteracting EP300 acetyltransferase activity, and repressing proximal gene expression. Furthermore, HDAC3 acts as a molecular chaperone, facilitating the shuttling of phosphorylated NR2C1 to PML bodies for sumoylation (By similarity). It contributes to NFE2L2-mediated HMOX1 transcription factor gene expression, promoting endothelial cell survival under disturbed flow and oxidative stress. In the circadian clock, HDAC3 regulates both activation and repression phases, influencing the ubiquitination of BMAL1, blocking FBXL3-mediated CRY1/2 ubiquitination, and promoting the interaction of CRY1 and BMAL1 (By similarity). As a versatile deacetylase, HDAC3 targets non-histone proteins like KAT5, MEF2D, MAPK14, and RARA, acting as a corepressor for RARA and mediating its deacetylation to inhibit RARE DNA element binding. Notably, HDAC3 also exhibits protein-lysine deacylase activity, removing acyl groups such as (2E)-butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) from lysine residues, contributing to protein decrotonylation and de-2-hydroxyisobutyrylation, respectively. This diverse range of activities highlights HDAC3's central role in epigenetic regulation and cellular processes.