Histone deacetylase 4 Recombinant Protein | HDAC4 recombinant protein

Recombinant Human Histone deacetylase 4

Cat. Num. AAA1265166

• Gene Names: HDAC4; HD4; AHO3; BDMR; HDACA; HA6116; HDAC-4; HDAC-A
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Histone deacetylase 4; Recombinant Human Histone deacetylase 4; HDAC4 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1-227aa; Partial
• Sequence: MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNH
• Sequence Length: 1084

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for HDAC4 recombinant protein

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.

Product Categories/Family for HDAC4 recombinant protein

Transcription

References

Three proteins define a class of human histone deacetylases related to yeast Hda1p.Grozinger C.M., Hassig C.A., Schreiber S.L.Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999) Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins.Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.DNA Res. 4:53-59(1997) Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. HDAC4 deacetylase associates with and represses the MEF2 transcription factor.Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T.EMBO J. 18:5099-5107(1999) HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor.Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., Th'ng J., Han J., Yang X.-J.Mol. Cell. Biol. 19:7816-7827(1999) Regulation of histone deacetylase 4 by binding of 14-3-3 proteins.Wang A.H., Kruhlak M.J., Wu J., Bertos N.R., Vezmar M., Posner B.I., Bazett-Jones D.P., Yang X.-J.Mol. Cell. Biol. 20:6904-6912(2000) The modular nature of histone deacetylase HDAC4 confers phosphorylation-dependent intracellular trafficking.Zhao X., Ito A., Kane C.D., Liao T.-S., Bolger T.A., Lemrow S.M., Means A.R., Yao T.-P.J. Biol. Chem. 276:35042-35048(2001) Identification of a signal-responsive nuclear export sequence in class II histone deacetylases.McKinsey T.A., Zhang C.-L., Olson E.N.Mol. Cell. Biol. 21:6312-6321(2001) The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases.Franco P.J., Farooqui M., Seto E., Wei L.-N.Mol. Endocrinol. 15:1318-1328(2001) The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase.Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.EMBO J. 21:2682-2691(2002) Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases.Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.Int. J. Cancer 121:265-275(2007) Nuclear calcium/calmodulin-dependent protein kinase IIdelta preferentially transmits signals to histone deacetylase 4 in cardiac cells.Little G.H., Bai Y., Williams T., Poizat C.J. Biol. Chem. 282:7219-7231(2007) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Haploinsufficiency of HDAC4 causes brachydactyly mental retardation syndrome, with brachydactyly type E, developmental delays, and behavioral problems.Williams S.R., Aldred M.A., Der Kaloustian V.M., Halal F., Gowans G., McLeod D.R., Zondag S., Toriello H.V., Magenis R.E., Elsea S.H.Am. J. Hum. 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NCBI and Uniprot Product Information

• NCBI GI #: 153085395
• NCBI GeneID: 9759
• NCBI Accession #: NP_006028.2
• NCBI GenBank Nucleotide #: NM_006037.3
• UniProt Accession #: P56524; Q86YH7; Q9UND6; E9PGB9; F5GX36
• Molecular Weight: 53.3 kDa
• NCBI Official Full Name: histone deacetylase 4
• NCBI Official Synonym Full Names: histone deacetylase 4
• NCBI Official Symbol: HDAC4
• NCBI Official Synonym Symbols: HD4; AHO3; BDMR; HDACA; HA6116; HDAC-4; HDAC-A
• NCBI Protein Information: histone deacetylase 4
• UniProt Protein Name: Histone deacetylase 4
• Protein Family: Histone deacetylase
• UniProt Gene Name: HDAC4
• UniProt Synonym Gene Names: KIAA0288; HD4
• UniProt Entry Name: HDAC4_HUMAN

NCBI Description

Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to class II of the histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. This protein does not bind DNA directly, but through transcription factors MEF2C and MEF2D. It seems to interact in a multiprotein complex with RbAp48 and HDAC3. [provided by RefSeq, Jul 2008]

Uniprot Description

HDAC4: a transcriptional regulator of the histone deacetylase family, subfamily 2. Deacetylates lysine residues on the N-terminal part of the core histones H2A, H2B, H3 AND H4. Plays an important role in transcriptional regulation, cell cycle progression and developmental events. Does not bind DNA directly, but through transcription factors MEF2C and MEF2D. It seems to interact in a multiprotein complex with RbAp48 and HDAC3.

Protein type: EC 3.5.1.98; Nuclear receptor co-regulator; Deacetylase; Hydrolase

Chromosomal Location of Human Ortholog: 2q37.3

Cellular Component: A band; actomyosin; cytoplasm; cytosol; histone deacetylase complex; neuromuscular junction; nucleoplasm; nucleus; transcriptional repressor complex; Z disc

Molecular Function: chromatin binding; histone deacetylase activity; histone deacetylase binding; NAD-dependent histone deacetylase activity (H3-K14 specific); potassium ion binding; protein binding; protein deacetylase activity; protein kinase binding; sequence-specific DNA binding; transcription activator binding; transcription corepressor activity; transcription factor binding; zinc ion binding

Biological Process: B cell activation; B cell differentiation; cardiac muscle hypertrophy; chromatin remodeling; histone deacetylation; inflammatory response; negative regulation of cell proliferation; negative regulation of glycolysis; negative regulation of osteoblast differentiation; negative regulation of transcription factor activity; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; nervous system development; osteoblast development; positive regulation of cell proliferation; positive regulation of neuron apoptosis; positive regulation of protein sumoylation; positive regulation of smooth muscle cell migration; positive regulation of smooth muscle cell proliferation; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; regulation of gene expression, epigenetic; regulation of protein binding; regulation of skeletal muscle fiber development; response to denervation involved in regulation of muscle adaptation; response to drug; skeletal development; transcription, DNA-dependent