|Application ||WB, IF|
|Predicted||Bovine, Chicken, Mouse, Monkey, Xenopus, Zebrafish|
|Calculated MW||29 KDa|
|Other Names||14-3-3 protein beta/alpha, Prepronerve growth factor RNH-1, Protein kinase C inhibitor protein 1, KCIP-1, 14-3-3 protein beta/alpha, N-terminally processed, Ywhab|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser58 conjugated to KLH.|
|Dilution||WB~~ 1:1000 |
|Format||Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.|
|Antibody Specificity||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.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-Ser58 14-3-3 Protein Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
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).
Berg D, Holzmann C, Riess O (2003) 14-3-3 Proteins in the nervous system. Nat Rev Neurosci 4:752-762.
Bridges D, Moorhead GB (2005) 14-3-3 Proteins: a number of functions for a numbered protein. Sci STKE 2005:re10.
Dougherty MK, Morrison DK (2004) Unlocking the code of 14-3-3. J Cell Sci 117:1875-1884.
Silhan J, Obsilova V, Vecer J, Herman P, Sulc M, Teisinger J, Obsil T (2004) 14-3-3 Protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding. J Biol Chem 279:49113-49119.
Woodcock JM, Murphy J, Stomski FC, Berndt MC, Lopez AF (2003) The dimeric versus monomeric status of 14-3-3 zeta is controlled by phosphorylation of Ser58 at the dimer interface. J Biol Chem 278:36323-36327.
Xiangjun Yang, Cheng Luo, Jian Cai, William M. Pierce, and Gülgün Tezel (2008) Phosphorylation-Dependent Interaction with 14-3-3 in the Regulation of Bad Trafficking in Retinal Ganglion Cells. Invest. Ophthalmol. Vis. Sci., 49: 2483 - 2494.
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