protein

Recombinant Human 14-3-3 protein eta

MBS1265389

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human 14-3-3 protein eta

14-3-3 protein eta

Protein AS1

14-3-3 protein eta; 14-3-3 protein eta; Protein AS1

YWHAH

YWHA1

YWHAH; YWHA1

1433F_HUMAN

E Coli

4-246

246

REQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDR
NLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEK
VKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYESK
VFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFE
ISKEQMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAK
QAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQ
QDEEAGEGN

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Signal Transduction

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.

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)

4507951

NP_003396.1

NM_003405.3

Q04917

55.3kD

Activation Of BAD And Translocation To Mitochondria Pathway (1270271); Activation Of BH3-only Proteins Pathway (1270270); Alpha6-Beta4 Integrin Signaling Pathway (198807); Apoptosis Pathway (1270262); Calcium Regulation In The Cardiac Cell Pathway (198906); Cell Cycle Pathway (1269741); Cell Cycle Checkpoints Pathway (1269742); Cell Cycle Pathway (198811); Cell Cycle Pathway (83054); Cell Cycle Pathway (463)

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

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180