Technical Data
0014-01B
14-3-3
Description:
14-3-3 proteins are a family of highly conserved proteins that appear to have multiple roles in cell signaling. The proteins are abundantly expressed in the brain and have been detected in the cerebrospinal fluid of patients with different neurological disorders. 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. The 14-3-3 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. (1-5)

Applications:
Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1,000. Detects a band of ~ 29kD.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
PabAffinity Purified
SizeStorageShippingSourceHost
100ul-20CBlue IceRatRabbit
Concentration:
Not determined
Immunogen:
Phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser58 of rat 14-3-3 protein.
Purity:
Purified by immunoaffinity chromatography.
Form
Supplied as a liquid in 10 mM Hepes, pH7.5, containing 150 mM NaCl, 100 ug/ml BSA and 50% glycerol.
Specificity:
Recognizes 14-3-3 protein. Species Crossreactivity: human, mouse, Xenopus, and rat based on 100% antigen sequence homology.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
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.