Phospho-p90RSK (Ser380) (D3H11) Rabbit Antibody

INQUIRY

CAT. NO.: AMA-0029

Target Information
UniProt ID	P51812

Product Details
Size	100 μL
Reactivity	Human, Monkey, Mouse, Rat, Mink
Host	Rabbit
Source/Isotype	Rabbit IgG
Storage	Store at -20°C.
Purification	Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser377 of human p90RSK3 protein.

Usage
Application	WB, IHC, IF
Product Usage Information Dilution	Western Blotting (1:1000); Immunohistochemistry (1:300); Immunofluorescence (1:800)
MW (Target)	90 kDa

Background
The 90 kDa ribosomal S6 kinases (RSK1-4) are a family of widely expressed Ser/Thr kinases characterized by two nonidentical, functional kinase domains and a carboxy-terminal docking site for extracellular signal-regulated kinases (ERKs). Several sites both within and outside of the RSK kinase domain, including Ser380, Thr359, Ser363, and Thr573, are important for kinase activation. RSK1-3 are activated via coordinated phosphorylation by MAPKs, autophosphorylation, and phosphoinositide-3-OH kinase (PI3K) in response to many growth factors, polypeptide hormones, and neurotransmitters.Upon mitogenic stimulation, p44/42 Erk1/2 and Erk5 MAP kinases cooperatively phosphorylate p90RSK at Thr573 (RSK1 numbering) located within the C-terminal kinase domain and at Thr359/Ser363 in the linker region between the two kinase domains. Phosphorylation at Thr573 within the activation loop of the p90RSK C-terminal kinase domain promotes activation and phosphorylation at Ser380 within the a hydrophobic stretch of the linker region. When phosphorylated, Ser380 acts as a docking site for the constitutively active Ser/Thr kinase PDK1, which in turn phosphorylates p90RSK at Ser221 within the N-terminal kinase domain activation loop, resulting in full enzymatic activation of p90RSK. Antibodies against these phosphorylation sites are useful for understanding the kinetics and regulation of p90RSK activation.

Background

The 90 kDa ribosomal S6 kinases (RSK1-4) are a family of widely expressed Ser/Thr kinases characterized by two nonidentical, functional kinase domains and a carboxy-terminal docking site for extracellular signal-regulated kinases (ERKs). Several sites both within and outside of the RSK kinase domain, including Ser380, Thr359, Ser363, and Thr573, are important for kinase activation. RSK1-3 are activated via coordinated phosphorylation by MAPKs, autophosphorylation, and phosphoinositide-3-OH kinase (PI3K) in response to many growth factors, polypeptide hormones, and neurotransmitters.Upon mitogenic stimulation, p44/42 Erk1/2 and Erk5 MAP kinases cooperatively phosphorylate p90RSK at Thr573 (RSK1 numbering) located within the C-terminal kinase domain and at Thr359/Ser363 in the linker region between the two kinase domains. Phosphorylation at Thr573 within the activation loop of the p90RSK C-terminal kinase domain promotes activation and phosphorylation at Ser380 within the a hydrophobic stretch of the linker region. When phosphorylated, Ser380 acts as a docking site for the constitutively active Ser/Thr kinase PDK1, which in turn phosphorylates p90RSK at Ser221 within the N-terminal kinase domain activation loop, resulting in full enzymatic activation of p90RSK. Antibodies against these phosphorylation sites are useful for understanding the kinetics and regulation of p90RSK activation.

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