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Key Documents

SRP5153

Sigma-Aldrich

14-3-3 ε, GST tagged human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Sinonimo/i:

14-3-3 ε, 14-3-3E, FLJ45465, KCIP-1, MDCR, MDS, YWHAE

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About This Item

Codice UNSPSC:
12352202
NACRES:
NA.32

Ricombinante

expressed in E. coli

Saggio

≥70% (SDS-PAGE)

Forma fisica

buffered aqueous glycerol solution

PM

~55 kDa

N° accesso NCBI

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

human ... YWHAE(7531)

Descrizione generale

14-3-3ε also known as tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein is a member of the 14-3-3 family. 14-3-3ε has been reported to be involved in heat shock transcription factor 1 (HSF1) and extracellular signal regulated protein kinase (ERK) pathways. 14-3-3ε interaction with the deubiquitinating enzyme UBPY, also known as USP8, regulates cargo sorting and membrane traffic at early endosomes. Association of 14-3-3ε, HSF1 with ERK during heat shock may modulate the amplitude of the response and control the termination of HSP expression on resumption of growth conditions.

Stato fisico

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

Nota sulla preparazione

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1


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Emi Mizuno et al.
Experimental cell research, 313(16), 3624-3634 (2007-08-28)
The deubiquitinating enzyme UBPY, also known as USP8, regulates cargo sorting and membrane traffic at early endosomes. Here we demonstrate the regulatory mechanism of the UBPY catalytic activity. We identified 14-3-3 epsilon, gamma, and zeta as UBPY-binding proteins using co-immunoprecipitation
Xiaozhe Wang et al.
The Journal of biological chemistry, 279(47), 49460-49469 (2004-09-15)
Cytoprotection during the heat shock response is a complex phenomenon involving multiple inducible mechanisms. We have examined the interaction of two key molecular components in the response, heat shock transcription factor 1 (HSF1) and extracellular signal regulated protein kinase (ERK).

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