12-331
Crosstide
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.42
eCl@ss:
32160405
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable (kinase)
shipped in
wet ice
Quality Level
Biochem/physiol Actions
Protein Target: MSK1
Target Sub-Family: AGC
Physical form
Lyophilized powder
Preparation Note
2 years at 4°C
Analysis Note
Routinely evaluated to phosphorylate MSK1, Akt/PKB, SGK or p70 S6 Kinase.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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.
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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
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)
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
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
D Konrad et al.
Diabetes, 50(6), 1464-1471 (2001-05-26)
The cofactor of mitochondrial dehydrogenase complexes and potent antioxidant alpha-lipoic acid has been shown to lower blood glucose in diabetic animals. alpha-Lipoic acid enhances glucose uptake and GLUT1 and GLUT4 translocation in 3T3-L1 adipocytes and L6 myotubes, mimicking insulin action.
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