- CITATIONS: 0
|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||28082 Da|
|Other Names||14-3-3 protein beta/alpha, Protein 1054, Protein kinase C inhibitor protein 1, KCIP-1, 14-3-3 protein beta/alpha, N-terminally processed, YWHAB|
|Target/Specificity||A synthetic peptide corresponding to C-terminal residues of human 14-3-3 b/a was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Function||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. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2.|
|Cellular Location||Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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Provided below are standard protocols that you may find useful for product applications.
The 14-3-3 proteins are a family of proteins involved in the regulation of apoptosis, mitogenic signaling and cell-cycle checkpoints (1). The 14-3-3 proteins are thought to be key regulators of signal transduction events mediated through their binding to serine-phosphorylated proteins (2,3). Through binding Bad, 14-3-3 prevents apoptosis by sequestering Bad to the cytosol (3).
1. Fu, H., et al. 14-3-3 proteins: structure, function, and regulation. Ann. Rev. Pharmacol. Toxicol. 40: 617
2. Muslin, A.J. et al. Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine. Cell 84: 889
3. Zha, J. et al. Serine Phosphorylation of Death Agonist BAD in Response to Survival Factor Results in Binding to 14-3-3 Not BCL-XL. Cell 87: 619
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