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SRP5154

Sigma-Aldrich

14-3-3 ε, untagged human

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

Synonym(s):

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

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About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

mol wt

~30 kDa

NCBI accession no.

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... YWHAE(7531)

General description

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.

Physical form

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

Preparation Note

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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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