Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 10 μl per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
Application References:
1. Johnson, J. D., et al., 2006. PNAS 103:19575. Pubmed
Hela cell extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with rabbit anti-14-3-3 ζ/δ antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system. This antibody detects the 14-3-3 ζ/δ protein (30 kD) as well as a protein of unknown identity with a molecular weight of approximately 60 kD.
Description:
The 30 kD 14-3-3 cytoplasmic protein participates in signal transduction by binding to phosphoserine-containing proteins and activating protein kinase C. This protein has also been shown to activate tyrosine/ tryptophan hydroxylases in presence of Ca2+/calmodulin-dependent protein kinase II, regulate insulin sensitivity, inhibit tuberin function, participate in actin cytoskeletal alterations, regulate cell adhesion, and inhibit the pro-apoptotic protein Bad. This protein forms dimers and can be modified by acetylation and phosphorylation. The δ isoform of 14-3-3 is phosphorylated on serine-185; phosphorylation disrupts dimerization. The 14-3-3 protein has been shown to interact with MAPKAPK2, IRS1, PKB/Akt, tuberin, cofilin, LIMK1, ADAM 22, and Bad proteins. The Poly6148 antibody has been shown to be useful for Western blotting of the mouse and human 14-3-3 proten.
Other Names:
Protein kinase C inhibitor protein-1, Phospholipase A2, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, zeta polypeptide (YWHAZ)
Structure:
14-3-3 protein superfamily, dimer, δ isoform is Ser185 phosphorylated; 30 kD
Distribution:
Cytoplasm
Function:
Mediates signal transduction by binding to phosphoserine-containing proteins. Activates PKC, tyrosine, tryptophan hydroxylases in presence of Ca2+/calmodulin-dependent protein kinase II. Regulates insulin sensitivity and cell adhesion. Inhibits
Regulation:
Phosphorylation disrupts dimerization
Modification:
Phosphorylation, Acetylation
Interaction:
MAPKAPK2, IRS1, PKB/Akt, tuberin, cofilin, LIMK1, ADAM 22, Bad
Antigen References:
1. Isobe, T., et al., 1992. FEBS Lett. 308:121. 2. Ogihara, T., et al., 1997. J. Biol. Chem. 272:25267. 3. Powell, D., et al., 2002. J. Biol. Chem. 277:21639. 4. Powell, D., et al., 2003. Mol. Cell Biol. 23:5376.
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