Product Name: 14-3-3 (phospho Ser58) Antibody
Species Reactivity: Bovine, Chicken, Dog, Human, Mouse, Rat, Sheep, Xenopus, Zebrafish
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.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 29
Immunogen: Phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser58 of rat 14-3-3 protein.
Host Species: Rabbit
Purification: Affinity Purified
Physical State: Liquid
CAS NO.: 19309-14-9
Product: Cardamonin
Buffer: 100 uL in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per mL BSA and 50% glycerol.
Concentration:
Storage Conditions: 14-3-3 antibody can be stored at -20˚C and is stable at -20˚C for at least 1 year.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: Prepronerve growth factor RNH-1, KCIP-1
Accession NO.: P35213
Protein Ino: 1345591
Official Symbol: Ywhab
Geneid: 56011
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 onserine 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).
PubMed ID:http://aac.asm.org/content/51/10/3672.abstract
