Histone deacetylase 7 (HDAC7) is a class IIa HDAC enzyme involved in epigenetic regulation by removing acetyl groups from histone proteins, leading to chromatin condensation and transcriptional repression. Unlike class I HDACs, HDAC7 shuttles between the nucleus and cytoplasm, modulating gene expression in coordination with cellular signaling pathways. It plays critical roles in development, differentiation, and disease processes, including cardiovascular formation, T-cell regulation, and cancer progression. HDAC7 interacts with transcription factors like MEF2 and FOXP3. influencing cell survival, metabolism, and immune responses.
HDAC7 antibodies are essential tools for studying its expression, localization, and function. They are widely used in techniques such as Western blotting, immunoprecipitation, immunofluorescence, and chromatin immunoprecipitation (ChIP). Due to high homology among class IIa HDACs, antibody specificity is crucial; validation often involves knockout controls or siRNA-mediated HDAC7 depletion. Commercial HDAC7 antibodies typically target unique epitopes within its N-terminal regulatory domain or C-terminal catalytic region.
Research applications include investigating HDAC7's role in tumorigenesis, where it may act as an oncogene or tumor suppressor depending on context, and exploring its therapeutic potential as a target for HDAC inhibitors. Antibodies also aid in studying post-translational modifications (e.g., phosphorylation) that regulate HDAC7 activity. Proper validation ensures reliable detection of the ~104 kDa protein across human, mouse, and rat samples.