|Application ||WB, IF|
|Calculated MW||119040 Da|
|Other Names||Histone deacetylase 4, HD4, HDAC4, KIAA0288|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human Histone Deacetylase 4 was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Histone Deactylase 4 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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).|
|Cellular Location||Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-246, Ser-467 and Ser-632 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation|
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Provided below are standard protocols that you may find useful for product applications.
Histone deacetylase 4 belongs to the histone deacetylase family type 2 which actively deacetylate the 4 core Histones . HDAC4 possesses two repression domains, one composed of the N-terminal 208 residues and the other consist of a deacetylase domain (1). The N-term will interact with the MADX-box of MEFC2 to negatively regulate expression. Additionally, the deacetylase activity of HDAC4 is subject to negative regulation by its N-terminal domain (2). HDAC4 is also implicated in the regulation of muscle differentiation. During muscle differentiation, HDC4 is shuttled between nuclear and cytoplasmic compartments. Phosphorylation by CAMK4 at S246, S467 and S632 can control HDAC4 subcellular localization (3-4).
1. Grunstein, M . 1997. Nature 389:349-352
2. Miska, E., C. Karlsson, E. Langley, S. Nielsen, J. Pines, and T. Kouzarides. EMBO J., in press
3. Lu, J., McKinsey, T. A., Nicol, R. L., and Olson, E. N. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 4070-4075
4. Xuan Zhao, Akihiro Ito, Christopher D. Kane, Ting-Sheng Liao, Timothy A. Bolger, Shannon M. Lemrow, Anthony R. Means, and Tso-Pang Yao, J. Biol. Chem., Vol. 276, Issue 37, 35042-35048, September 14, 2001.
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