Chromodomain-helicase-DNA-binding protein 4 Recombinant Protein | CHD4 recombinant protein

Recombinant Human Chromodomain-helicase-DNA-binding protein 4

Cat. Num. AAA1265609

• Gene Names: CHD4; CHD-4; Mi-2b; Mi2-BETA
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Chromodomain-helicase-DNA-binding protein 4; Recombinant Human Chromodomain-helicase-DNA-binding protein 4; ATP-dependent helicase CHD4; Mi-2 autoantigen 218 kDa protein; Mi2-beta; CHD4 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: 1-219aa; Partial
• Sequence: MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKERMLLCRQLGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFK
• Sequence Length: 1912

• 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 CHD4 recombinant protein

Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.

Product Categories/Family for CHD4 recombinant protein

Epigenetics and Nuclear Signaling

References

The major dermatomyositis specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation.Seelig H.P., Moosbrugger I., Ehrfeld H., Fink T., Renz M., Genth E.Arthritis Rheum. 38:1389-1399(1995) The finished DNA sequence of human chromosome 12.Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.Nature 440:346-351(2006) Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex.Tong J.K., Hassig C.A., Schnitzler G.R., Kingston R.E., Schreiber S.L.Nature 395:917-921(1998) Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4.Schmidt D.R., Schreiber S.L.Biochemistry 38:14711-14717(1999) Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes.Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.Immunity 10:345-355(1999) Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities.Shimono Y., Murakami H., Kawai K., Wade P.A., Shimokata K., Takahashi M.J. Biol. Chem. 278:51638-51645(2003) MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation.Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.Cell 119:75-86(2004) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) Chromatin remodeling proteins interact with pericentrin to regulate centrosome integrity.Sillibourne J.E., Delaval B., Redick S., Sinha M., Doxsey S.J.Mol. Biol. Cell 18:3667-3680(2007) ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.Science 316:1160-1166(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) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) ZIP a novel transcription repressor, represses EGFR oncogene and suppresses breast carcinogenesis.Li R., Zhang H., Yu W., Chen Y., Gui B., Liang J., Wang Y., Sun L., Yang X., Zhang Y., Shi L., Li Y., Shang Y.EMBO J. 28:2763-2776(2009) 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) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3.Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.Mol. Cell. Biol. 31:2641-2652(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) Senataxin, defective in the neurodegenerative disorder ataxia with oculomotor apraxia 2, lies at the interface of transcription and the DNA damage response.Yuce O., West S.C.Mol. Cell. Biol. 33:406-417(2013) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Engineering a protein scaffold from a PHD finger.Kwan A.H.Y., Gell D.A., Verger A., Crossley M., Matthews J.M., Mackay J.P.Structure 11:803-813(2003) Solution structures of the chromo domain of human chromodomain helicase-DNA-binding protein 4.RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bank

NCBI and Uniprot Product Information

• NCBI GI #: 51599156
• NCBI GeneID: 1108
• NCBI Accession #: NP_001264.2
• NCBI GenBank Nucleotide #: NM_001273.3
• UniProt Accession #: Q14839; Q8IXZ5
• Molecular Weight: 31.8 kDa
• NCBI Official Full Name: chromodomain-helicase-DNA-binding protein 4 isoform 1
• NCBI Official Synonym Full Names: chromodomain helicase DNA binding protein 4
• NCBI Official Symbol: CHD4
• NCBI Official Synonym Symbols: CHD-4; Mi-2b; Mi2-BETA
• NCBI Protein Information: chromodomain-helicase-DNA-binding protein 4
• UniProt Protein Name: Chromodomain-helicase-DNA-binding protein 4
• Protein Family: Chromodomain-helicase-DNA-binding protein
• UniProt Gene Name: CHD4
• UniProt Synonym Gene Names: CHD-4
• UniProt Entry Name: CHD4_HUMAN

NCBI Description

The product of this gene belongs to the SNF2/RAD54 helicase family. It represents the main component of the nucleosome remodeling and deacetylase complex and plays an important role in epigenetic transcriptional repression. Patients with dermatomyositis develop antibodies against this protein. Somatic mutations in this gene are associated with serous endometrial tumors. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2014]

Uniprot Description

CHD-4: is an ATP-dependent helicase and a central component of the HDAC-containing nucleosome remodeling and histone deacetylase (NuRD) transcriptional complex. Interacts with MTA1/2, HDAC1, and RbAp46 in the NuRD complex. CHD-4 belongs to the SNF2/RAD54 helicase family of proteins. The NuRD complex, whose subunit composition varies by cell type and in response to physiologic signals, plays central roles in many processes including oncogenesis and metastasis, B cell differentiation, invasive growth of breast cancer, and maintaining the balance between the undifferentiated state and the process of differentiation in embryonic stem cells.

Protein type: Helicase; EC 3.6.4.12; DNA-binding

Chromosomal Location of Human Ortholog: 12p13

Cellular Component: centrosome; cytoplasm; membrane; nuclear chromatin; nucleoplasm; nucleus; NuRD complex; protein complex

Molecular Function: ATP binding; ATP-dependent DNA helicase activity; DNA binding; microtubule binding; nucleosomal DNA binding; protein binding; zinc ion binding

Biological Process: ATP-dependent chromatin remodeling; DNA duplex unwinding; establishment and/or maintenance of chromatin architecture; negative regulation of transcription from RNA polymerase II promoter; regulation of transcription from RNA polymerase II promoter; spindle assembly; transcription, DNA-dependent