Product Pathways - MAPK Signaling
Phospho-p90RSK (Ser380) (D3H11) Rabbit mAb #11989
|11989S||100 µl (10 western blots)||---||In Stock||---|
|11989||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey, Mink||Endogenous||90||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IHC-P=Immunohistochemistry (Paraffin), IF-IC=Immunofluorescence (Immunocytochemistry)
Species predicted to react based on 100% sequence homology: Chicken, Xenopus, Zebrafish, Bovine, Dog, Pig, Horse.
Specificity / Sensitivity
Phospho-p90RSK (Ser380) (D3H11) Rabbit mAb recognizes endogenous levels of p90RSK1 protein when phosphorylated at Ser380. This antibody also detects p90RSK2 phosphorylated at Ser386 and p90RSK3 phosphorylated at Ser377.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser377 of human p90RSK3 protein.
Western blot analysis of extracts from various cell lines, starved overnight and either untreated (-) or treated (+) with TPA #4174 (200 nM, 15 min), Human Epidermal Growth Factor (hEGF) #8916 (100 ng/mL, 15 min), or Human Platelet-Derived Growth Factor BB (hPDGF-BB) #8912 (100 ng/mL, 15 min) as indicated, using Phospho-p90RSK (Ser380) (D3H11) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human colon carcinoma, control (left) or λ phosphatase-treated (right), using Phospho-p90RSK (Ser380) (D3H11) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human ovarian carcinoma using Phospho-p90RSK (Ser380) (D3H11) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded HeLa cell pellets, untreated (left) or treated with TPA #4174 (right), using Phospho-p90RSK (Ser380) (D3H11) Rabbit mAb.
Confocal immunofluorescent analysis of NIH/3T3 cells, serum-starved (left), treated with TPA #4174 (200 nM, 15 min; center), or treated with TPA followed by λ phosphatase (right), using Phospho-p90RSK (Ser380) (D3H11) Rabbit mAb (green). Actin filaments were labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
The 90 kDa ribosomal S6 kinases (RSK1-4) are a family of widely expressed Ser/Thr 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, autophosphorylation, and phosphoinositide-3-OH kinase (PI3K) in response to many growth factors, polypeptide hormones, and neurotransmitters (3).
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 (3). 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 (4,5). 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 (6). Antibodies against these phosphorylation sites are useful for understanding the kinetics and regulation of p90RSK activation.
For more information regarding the phospho-regulatory sites within each p90RSK isoform, including more information regarding the seminal studies demonstrating the complex phosphorylation cascades involved, please see the references herein and PhosphoSitePlus® (www.phosphosite.org).
- Fisher, T.L. and Blenis, J. (1996) Mol Cell Biol 16, 1212-9.
- Smith, J.A. et al. (1999) J Biol Chem 274, 2893-8.
- Dalby, K.N. et al. (1998) J Biol Chem 273, 1496-505.
- Roux, P.P. et al. (2003) Mol Cell Biol 23, 4796-804.
- Cargnello, M. and Roux, P.P. (2011) Microbiol Mol Biol Rev 75, 50-83.
- Romeo, Y. et al. (2012) Biochem J 441, 553-69.
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