14-3-3 (phospho Ser58) Antibody Cat. No.: 50-231

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psi-iconSpecifications
HOST SPECIES:Rabbit
SPECIES REACTIVITY: Bovine, Chicken, Dog, Human, Mouse, Rat, Sheep, Xenopus, Zebrafish
IMMUNOGEN: Phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser58 of rat 14-3-3 protein.
TESTED APPLICATIONS: IHC, WB
APPLICATIONS: The antibody has been directly tested for reactivity in Western blots with human and rat tissue. It is anticipated that the antibody will react with bovine, canine, chicken, mouse, non-human primates, sheep, Xenopus and zebra fish based on the fact that these species have 100% homology with the amino acid sequence used as antigen for this antibody.
PREDICTED MOLECULAR WEIGHT: 29

psi-iconProperties
PURIFICATION:Affinity Purified
CLONALITY:Polyclonal
CONJUGATE:Unconjugated
PHYSICAL STATE:Liquid
BUFFER:100 uL in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per mL BSA and 50% glycerol.
STORAGE CONDITIONS:14-3-3 antibody can be stored at -20˚C and is stable at -20˚C for at least 1 year.

psi-iconAdditional Info
OFFICIAL SYMBOL:Ywhab
ALTERNATE NAMES:Prepronerve growth factor RNH-1, KCIP-1
ACCESSION NO.:P35213
PROTEIN GI NO.:1345591
GENE ID:56011
USER NOTE:Optimal dilutions for each application to be determined by the researcher.
psi-iconBackground and References
BACKGROUND: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).
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.

ANTIBODIES FOR RESEARCH USE ONLY.

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