manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable (kinase)
shipped in
wet ice
Quality Level
Analysis Note
Routinely evaluated to phosphorylate MSK1, Akt/PKB, SGK or p70 S6 Kinase.
Biochem/physiol Actions
Protein Target: MSK1
Target Sub-Family: AGC
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Physical form
Lyophilized powder
Preparation Note
2 years at 4°C
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
G Sweeney et al.
The Journal of biological chemistry, 274(15), 10071-10078 (1999-04-03)
The precise mechanisms underlying insulin-stimulated glucose transport still require investigation. Here we assessed the effect of SB203580, an inhibitor of the p38 MAP kinase family, on insulin-stimulated glucose transport in 3T3-L1 adipocytes and L6 myotubes. We found that SB203580, but
M L Standaert et al.
The Journal of biological chemistry, 274(36), 25308-25316 (1999-08-28)
In rat adipocytes, insulin provoked rapid increases in (a) endogenous immunoprecipitable combined protein kinase C (PKC)-zeta/lambda activity in plasma membranes and microsomes and (b) immunoreactive PKC-zeta and PKC-lambda in GLUT4 vesicles. Activity and autophosphorylation of immunoprecipitable epitope-tagged PKC-zeta and PKC-lambda
Oxidative stress impairs insulin but not platelet-derived growth factor signalling in 3T3-L1 adipocytes
Tirosh, A., et al
The Biochemical Journal, 355, 757-763 (2001)
R Somwar et al.
The Biochemical journal, 359(Pt 3), 639-649 (2001-10-24)
We previously reported that SB203580, an inhibitor of p38 mitogen-activated protein kinase (p38 MAPK), attenuates insulin-stimulated glucose uptake without altering GLUT4 translocation. These results suggested that insulin might activate GLUT4 via a p38 MAPK-dependent pathway. Here we explore this hypothesis
Satoru Takahashi et al.
The Journal of biological chemistry, 278(33), 30821-30827 (2003-06-12)
Endothelial nitric-oxide synthase (eNOS), which generates the endogenous vasodilator, nitric oxide (NO), is highly regulated by post-translational modifications and protein interactions. We recently used purified proteins to characterize the mechanisms by which heat shock protein 90 (HSP90) increases eNOS activity
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