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p38/SAPK2 Inhibitor (SB 203580)
The p38/SAPK2 Inhibitor (SB 203580) controls the biological activity of p38/SAPK2. This small molecule/inhibitor is primarily used for Biochemicals applications.
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About This Item
UNSPSC Code:
12352200
eCl@ss:
32160405
NACRES:
NA.41
Recommended Products
Quality Level
form
solid
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable (kinase)
NCBI accession no.
UniProt accession no.
shipped in
wet ice
Application
Highly specific inhibitor of p38/SAPK2
Biochem/physiol Actions
Inhibitor Type: Kinase
Protein Target: p38/SAPK2
Target Sub-Family: CMGC
Quality
Routinely evaluated in a kinase assay.
Physical form
C12H16FN3OS
Storage and Stability
3 years at -20°C
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.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 4 Oral
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Pharmacological profile of SB 203580, a selective inhibitor of cytokine suppressive binding protein/p38 kinase, in animal models of arthritis, bone resorption, endotoxin shock and immune function.
Badger, A M, et al.
Journal of Pharmacology and Experimental Therapeutics, 279, 1453-1461 (1996)
p38/RK is essential for stress-induced nuclear responses: JNK/SAPKs and c-Jun/ATF-2 phosphorylation are insufficient.
Hazzalin, C A, et al.
Current Biology, 6, 1028-1031 (1996)
R M Kramer et al.
The Journal of biological chemistry, 271(44), 27723-27729 (1996-11-01)
The Ca2+-sensitive 85-kDa cytosolic phospholipase A2 (cPLA2) is responsible for thrombin-stimulated mobilization of arachidonic acid for the synthesis of thromboxane A2 in human platelets. We have previously shown that thrombin activates p38 kinase, a recently discovered new member of the
J Saklatvala et al.
The Journal of biological chemistry, 271(12), 6586-6589 (1996-03-22)
p38 mitogen-activated protein kinase (MAPK) was identified in platelets on the basis of (a) its reactivity with antibodies to C-terminal and N-terminal peptides, and (b) its ability to activate MAPK-activated protein kinase-2, which phosphorylates the small heat shock protein, hsp27.
Liangxuan Zhang et al.
Infection and immunity, 72(1), 38-45 (2003-12-23)
Our previous studies showed that bacterial heat shock protein 60 (hsp60) induces cultured epithelial cell proliferation within 24 h. Here we investigated the long-term effects of heat shock protein 60 isolated from Actinobacillus actinomycetemcomitans on skin keratinocyte (HaCaT cell line)
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