Recombinant human HDAC4 protein is a Human Fragment protein, in the 612 to 1084 aa range, expressed in Baculovirus infected Sf9, with >95% purity and suitable for SDS-PAGE, FuncS.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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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 via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1 (PubMed:27708256).
KIAA0288, HDAC4, Histone deacetylase 4, HD4
Recombinant human HDAC4 protein is a Human Fragment protein, in the 612 to 1084 aa range, expressed in Baculovirus infected Sf9, with >95% purity and suitable for SDS-PAGE, FuncS.
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.307% Glutathione, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00292% EDTA, 0.00174% PMSF
Purity was determined to be >95% by densitometry. Affinity purified.
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 via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1 (PubMed:27708256).
Belongs to the histone deacetylase family. HD type 2 subfamily.
Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-350, within the PxLPxI/L motif, impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
HDAC4 also known as Histone Deacetylase 4 functions in the regulation of gene expression through chromatin remodeling. This protein removes acetyl groups from histone proteins causing chromatin compaction and transcriptional repression. HDAC4 has a molecular weight of approximately 140 kDa. The protein is found in various tissues including brain heart and skeletal muscle and plays essential roles in various cellular processes. Alternate names for HDAC4 include KIAA0288 and HD4.
The role of HDAC4 extends beyond chromatin remodeling as it serves as a critical regulator in several cellular functions. As part of a complex HDAC4 interacts with other proteins to control cell cycle differentiation and apoptosis. It cooperates with transcriptional repressors like MEF2 and RUNX2 influencing various signaling pathways. The protein's activity impacts neuronal survival muscle development and cardiac hypertrophy through its regulatory mechanisms.
HDAC4 integrates into significant signaling networks notably the MAPK and calcium-calmodulin signaling pathways. Within the MAPK pathway HDAC4 associates with proteins like MEF2 impacting cellular growth and differentiation processes. In the calcium-calmodulin pathway HDAC4 affects gene transcription via its interaction with the phosphatase calcineurin linking intracellular calcium levels with transcriptional responses.
HDAC4 has associations with neurological disorders and cancer. Mutations and dysregulation in HDAC4 are linked to neuronal disorders such as Huntington's disease. In cancer HDAC4 interacts with other oncogenic proteins such as p53 influencing tumor progression and resistance to therapy. Consequently HDAC4 presents as a potential target for therapeutic intervention in these disease contexts.
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Kinase Assay demonstrating specific activity of ab104029.
SDS-PAGE showing ab104029 at approximately 77kDa.
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