Histone acetyltransferase 1 (HAT1), a member of the GNAT (GCN5-related N-acetyltransferase) superfamily, is responsible for catalyzing the acetylation of histone H4 on lysine residues, particularly during chromatin assembly and nucleosome remodeling. It plays a critical role in epigenetic regulation by modulating chromatin structure and gene expression. HAT1 primarily acetylates free histone H4 but may also interact with other histones or non-histone proteins. Its activity is tightly linked to DNA replication and repair, cell cycle progression, and cellular differentiation.
HAT1 antibodies are essential tools for studying its expression, localization, and function in these processes. They are widely used in techniques like Western blotting, immunoprecipitation, immunofluorescence, and chromatin immunoprecipitation (ChIP). Researchers employ these antibodies to explore HAT1's involvement in diseases such as cancer, where dysregulated acetylation contributes to oncogenesis, or in developmental disorders linked to epigenetic aberrations. Some studies also investigate its interaction with chaperones (e.g., ASF1B) during histone deposition. Commercial HAT1 antibodies are typically raised against specific epitopes, often validated for cross-reactivity and species specificity (e.g., human, mouse). Recent work highlights its dual role in cytoplasmic histone acetylation and potential nuclear functions, making these antibodies vital for dissecting context-dependent regulatory mechanisms.