The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/500 - 1/1000. Detects a band of approximately 118 kDa (predicted molecular weight: 122 kDa).
Use at an assay dependent concentration.
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors.
Belongs to the histone deacetylase family. HD type 2 subfamily.
The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.
Phosphorylated by CaMK at Ser-259 and Ser-498. The phosphorylation is required for the export to the cytoplasm. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Ubiquitinated. Polyubiquitination however does not lead to its degradation.
Nucleus. Cytoplasm. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-259 and Ser-498 by CaMK.
Weeks KL et al. ß-Adrenergic Stimulation Induces Histone Deacetylase 5 (HDAC5) Nuclear Accumulation in Cardiomyocytes by B55a-PP2A-Mediated Dephosphorylation. J Am Heart Assoc6:N/A (2017).
Read more (PubMed: 28343149) »
Yuan SY et al. AMPK Mediates Glucocorticoids Stress-Induced Downregulation of the Glucocorticoid Receptor in Cultured Rat Prefrontal Cortical Astrocytes. PLoS One11:e0159513 (2016).
Read more (PubMed: 27513844) »