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Chromodomain-Helicase-DNA-Binding Protein 4 (CHD4) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS1265609

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

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Product Overview

Product Name
Chromodomain-helicase-DNA-binding protein 4 (CHD4), Recombinant Protein
Full Product Name
Recombinant Human Chromodomain-helicase-DNA-binding protein 4
Product Gene Name
Product Synonym Names
ATP-dependent helicase CHD4; Mi-2 autoantigen 218 kDa protein; Mi2-beta
Sequence
MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPE EDLSETETPK LKKKKKPKKP RDPKIPKSKR QKKERMLLCR QLGDSSGEGP EFVEEEEEVA LRSDSEGSDY TPGKKKKKKL GPKKEKKSKS KRKEEEEEED DDDDSKEPKS SAQLLEDWGM EDIDHVFSEE DYRTLTNYKA FSQFVRPLIA AKNPKIAVSK MMMVLGAKWR EFSTNNPFK
Host
E Coli
Form/Format
Liquid containing glycerol
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
31.8 kDa
Sequence Positions
1-219aa; Partial
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
603277
3D Structure
ModBase 3D Structure for Q14839
ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for CHD4 recombinant protein

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

Other Notes

Small volumes of CHD4 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for CHD4 purchase

MBS1265609 is a recombinant protein targeting CHD4. Also known as Recombinant Human Chromodomain-helicase-DNA-binding protein 4. Host: E Coli.

Additional Details

NCBI/Uniprot data below describe general gene information for CHD4. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
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
UniProt Protein Name
Chromodomain-helicase-DNA-binding protein 4
UniProt Synonym Protein Names
ATP-dependent helicase CHD4; Mi-2 autoantigen 218 kDa protein; Mi2-beta
UniProt Gene Name
CHD4
UniProt Synonym Gene Names
CHD-4
UniProt Entry Name
CHD4_HUMAN
NCBI Protein Information
chromodomain-helicase-DNA-binding protein 4

NCBI Summary for CHD4

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]
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UniProt Comments for CHD4

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
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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