14-3-3 (phospho Ser58) Antibody | 50-231

14-3-3 (phospho Ser58) Antibody | 50-231 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Mouse, Rat, Dog, Zebrafish, Sheep, Bovine, Chicken, Frog

Homology: N/A

Immunogen: Phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser58 of rat 14-3-3 protein.

Research Area: Phospho-Specific

Tested Application: WB, IHC

Application: 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.

Specificiy: N/A

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 29

Validation: N/A

Isoform: N/A

Purification: Affinity Purified

Clonality: Polyclonal

Clone: N/A

Isotype: N/A

Conjugate: Unconjugated

Physical State: Liquid

Buffer: N/A

Concentration: N/A

Storage Condition: 14-3-3 antibody can be stored at -20˚C and is stable at -20˚C for at least 1 year.

Alternate Name: N/A

User Note: Optimal dilutions for each application to be determined by the researcher.

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) .