Phospho-p90RSK (Thr359) (D1E9) Rabbit mAb #8753
- WB
- IP
- IHC
- IF
Supporting Data
| REACTIVITY | H R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 90 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Immunohistochemistry (Paraffin) | 1:50 - 1:200 |
| Immunofluorescence (Immunocytochemistry) | 1:50 - 1:100 |
Storage
For a carrier-free (BSA and azide free) version of this product see product #55773.
Protocol
Specificity / Sensitivity
Species Reactivity:
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Source / Purification
Background
Upon mitogenic stimulation, p44/42 Erk1/2 and Erk5 MAP kinases cooperatively phosphorylate p90RSK at Thr573 (p90RSK1 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 directs phosphorylation at Ser380 within the 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 RSK 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.
Limited Uses
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