14-3-3, phosphorylated (Ser58)

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).\n\nApplications:\nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nWestern Blot: 1:1000\nOptimal dilutions to be determined by the researcher.\n\nPositive Control:\nRat brainstem lysate\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

0014-01Q

Size

100ul

Applications

WB

Hosts

Rabbit

Reactivities

Rat

Form

Supplied as a liquid 10mM HEPES, pH 7.5, 150mM sodium chloride, 100ug per ml BSA, 50% glycerol.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

Isotype

IgG

References

1. Berg D, Holzmann C, Riess O (2003) 14-3-3 Proteins in the nervous system. Nat Rev Neurosci 4:752-762. 2. Bridges D, Moorhead GB (2005) 14-3-3 Proteins: a number of functions for a numbered protein. Sci STKE 2005:re10. 3. Dougherty MK, Morrison DK (2004) Unlocking the code of 14-3-3. J Cell Sci 117:1875-1884. 4. 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. 5. 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.

Additional Info

Recognizes rat 14-3-3, phosphorylated (Ser58). Species Sequence Homology: human and mouse.