Specific for the ~29k 14-3-3 protein phosphorylated at Ser58. Immunolabeling is blocked by the phosphopeptide used as antigen but not by the corresponding dephosphopeptide.
Réactivité croisée
Humain, Rat (Rattus)
Homologie
bovine, canine, chicken, mouse, non-human primates, sheep, Xenopus, zebra fish
Purification
Antigen Affinity Purified from Pooled Serum
Immunogène
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser58 conjugated to KLH
14-3-3 proteins are a family of highly conserved proteins that appear to have multiple roles in cell signaling (Bridges and Moorhead, 2005). The proteins are abundantly expressed in the brain and have been detected in the cerebrospinal fluid of patients with different neurological disorders (Berg et al., 2003). 14-3-3 proteins bind protein ligands that are typically phosphorylated on serine or threonine residues and regulate the functions of these binding partners by a number of different mechanisms (Silhan et al., 2004, Dougherty and Morrison, 2004). The14-3-3 proteins affect a diverse array of cellular processes including the cell cycle and transcription, signal transduction and intracellular trafficking. These functions of 14-3-3 proteins are facilitated by, if not dependent on, its dimeric structure. Recent work has demonstrated that the dimeric status of the 14-3-3 protein is regulated by site-specific serine phosphorylation (Woodcock et al., 2003). Anti-Phospho-Ser58 14-3-3 Protein Western blot of rat brainstem lysate showing specific immuno- labeling of the ~29k 14-3-3 protein phosphorylated at Ser58 (Control). The immunolabeling is blocked by the phosphopeptide used as the antigen (Phos-pep) but not by the corresponding dephosphopeptide (not shown).