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YWHAH recombinant protein :: 14-3-3 protein eta Recombinant Protein

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Catalog # MBS1265389
Unit / Price
  0.01 mg  /  $160 +1 FREE 8GB USB
  0.05 mg  /  $200 +1 FREE 8GB USB
  0.1 mg  /  $295 +1 FREE 8GB USB
  0.2 mg  /  $480 +1 FREE 8GB USB
  0.5 mg  /  $790 +1 FREE 8GB USB
  1 mg  /  $1,215 +1 FREE 8GB USB
SDS-PAGE
Product Name

14-3-3 protein eta (YWHAH), Recombinant Protein

Popular Item
Full Product Name

Recombinant Human 14-3-3 protein eta

Product Synonym Names
Protein AS1
Product Synonym Gene Name
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
4-246aa; Partial
Sequence
REQLLQRARL AEQAERYDDM ASAMKAVTEL NEPLSNEDRN LLSVAYKNVV GARRSSWRVI SSIEQKTMAD GNEKKLEKVK AYREKIEKEL ETVCNDVLSL LDKFLIKNCN DFQYESKVFY LKMKGDYYRY LAEVASGEKK NSVVEASEAA YKEAFEISKE QMQPTHPIRL GLALNFSVFY YEIQNAPEQA CLLAKQAFDD AIAELDTLNE DSYKDSTLIM QLLRDNLTLW TSDQQDEEAG EGN
OMIM
113508
3D Structure
ModBase 3D Structure for Q04917
Host
E Coli
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
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.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of YWHAH 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.
Related Product Information for
YWHAH recombinant protein
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.
Product Categories/Family for YWHAH recombinant protein

YWHAH recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for YWHAH. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
Molecular Weight
55.3kD
NCBI Official Full Name
14-3-3 protein eta
UniProt Protein Name
14-3-3 protein eta
UniProt Synonym Protein Names
Protein AS1
Protein Family
UniProt Gene Name
YWHAH  [Similar Products]
UniProt Synonym Gene Names
YWHA1  [Similar Products]
UniProt Entry Name
1433F_HUMAN
UniProt Comments for YWHAH
14-3-3 eta: a protein of the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. A multifunctional regulator of the cell signaling processes.

Protein type: Nuclear receptor co-regulator; Adaptor/scaffold

Chromosomal Location of Human Ortholog: 22q12.3

Cellular Component: cytoplasm; cytoplasmic vesicle membrane; cytosol; mitochondrion; plasma membrane

Molecular Function: actin binding; enzyme binding; glucocorticoid receptor binding; insulin-like growth factor receptor binding; protein binding; protein domain specific binding; protein heterodimerization activity; sodium channel regulator activity

Biological Process: apoptosis; gene expression; glucocorticoid catabolic process; glucocorticoid receptor signaling pathway; intracellular protein transport; negative regulation of dendrite morphogenesis; positive regulation of transcription, DNA-dependent; programmed cell death; regulation of neuron differentiation; regulation of sodium ion transport; regulation of synaptic plasticity; small GTPase mediated signal transduction; substantia nigra development; transcription initiation from RNA polymerase II promoter
Product References and Citations for YWHAH recombinant protein
The human and bovine 14-3-3 eta protein mRNAs are highly conserved in both their translated and untranslated regions.Swanson K.D., Dhar M.S., Joshi J.G.Biochim. Biophys. Acta 1216:145-148(1993) cDNA cloning and chromosome assignment of the gene for human brain 14-3-3 protein eta chain.Ichimura-Ohshima Y., Morii K., Ichimura T., Araki K., Takahashi Y., Isobe T., Minoshima S., Fukuyama R., Shimizu N., Kuwano R.J. Neurosci. Res. 31:600-605(1992) Leffers H., Tommerup N., Celis J.E.The effect on methamphetamine on the mRNA level for 14.3.3 eta chain in the human cultured cells.Muratake T., Hayashi S., Ichimura Y., Morii K., Kuwano R., Ichikawa T., Kumanishi T., Isobe T., Watanabe M., Kondo H.Mol. Neurobiol. 11:223-230(1995) Structural organization and chromosomal assignment of the human 14-3-3 eta chain gene (YWHAH) .Muratake T., Hayashi S., Ichikawa T., Kumanishi T., Ichimura Y., Kuwano R., Isobe T., Wang Y., Minoshima S., Shimizu N., Takahashi Y.Genomics 36:63-69(1996) A genome annotation-driven approach to cloning the human ORFeome.Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.Genome Biol. 5:R84.1-R84.11(2004) The DNA sequence of human chromosome 22.Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.Nature 402:489-495(1999) Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway.Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E., Vandekerckhove J., Celis J.E.J. Mol. Biol. 231:982-998(1993) Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.Nat. Biotechnol. 21:566-569(2003) Bienvenut W.V.Submitted (AUG-2005) to UniProtKB Regulation of glucocorticoid receptor activity by 14-3-3-dependent intracellular relocalization of the corepressor RIP140.Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.Mol. Endocrinol. 15:501-511(2001) Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3.Sato S., Fujita N., Tsuruo T.J. Biol. Chem. 277:39360-39367(2002) Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization.Fujita N., Sato S., Tsuruo T.J. Biol. Chem. 278:49254-49260(2003) JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage.Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.Nat. Cell Biol. 7:278-285(2005) Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein.Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.EMBO J. 27:2305-2316(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) 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) 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) Structural basis for protein-protein interactions in the 14-3-3 protein family.Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006)

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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.

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