Phospho-p90RSK (Thr359/Ser363) Antibody detects endogenous levels of p90RSK only when phosphorylated at Thr359/Ser363. This antibody does not recognize p90RSK phosphorylated at other sites. It shows some cross-reactivity with RSK3 when phosphorylated at the homologous sites, but no cross-reactivity with phospho-RSK2 or -MSK1.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr359/Ser363 of rat RSK1. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The 90 kDa ribosomal S6 kinases (RSK1-4) are a family of widely expressed serine/threonine kinases characterized by two nonidentical, functional kinase domains (1) and a carboxy-terminal docking site for extracellular signal-regulated kinases (ERKs) (2). Several sites both within and outside of the RSK kinase domain, including Ser380, Thr359, Ser363, and Thr573, are important for kinase activation (3). RSK1-3 are activated via coordinated phosphorylation by MAPKs, by autophosphorylation, and by phosphoinositide-3-OH kinase (PI3K) in response to many growth factors, polypeptide hormones, and neurotransmitters (3).