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 delta 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.