SRP5158
14-3-3 θ, untagged human
recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
14-3-3, 14-3-3 θ, 1C5, HS1, YWHAQ
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About This Item
UNSPSC Code:
12352202
NACRES:
NA.32
recombinant
expressed in E. coli
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~29 kDa
NCBI accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... YWHAQ(10971)
General description
14-3-3θ (also known as tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, theta polypeptide) is a member of the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. Through interaction with ASK1, c-jun NH-terminal kinase, and p38 mitogen-activated protein kinase (MAPK), 14-3-3θ plays an important role in controlling apotopsis. Induced expression of 14-3-3θ protein has been reported in patients with amyotrophic lateral sclerosis. Additionally, 14-3-3θ has been observed to mediate nucleocytoplasmic shuttling of the N protein (coronavirus nucleocapsid protein) which causes severe acute respiratory syndrome.
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 Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Jeffrey M C Lau et al.
Molecular and cellular biology, 27(4), 1455-1466 (2006-12-06)
14-3-3 family members are intracellular dimeric phosphoserine-binding proteins that regulate signal transduction, cell cycle, apoptotic, and metabolic cascades. Previous work with global 14-3-3 protein inhibitors suggested that these proteins play a critical role in antagonizing apoptotic cell death in response
Milan Surjit et al.
Journal of virology, 79(17), 11476-11486 (2005-08-17)
The severe acute respiratory syndrome coronavirus(SARS-CoV) nucleocapsid (N) protein is one of the four structural proteins of the virus and is predicted to be a 46-kDa phosphoprotein. Our in silico analysis predicted N to be heavily phosphorylated at multiple residues.
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