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p38/SAPK2 Inhibitor (SB 202190)
The p38/SAPK2 Inhibitor (SB 202190) 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
Potent inhibitor of p38 alpha/SAPK2a and p38 beta/SAPK2b kinases.
The p38/SAPK2 Inhibitor (SB 202190) controls the biological activity of p38/SAPK2. This small molecule/inhibitor is primarily used for Biochemicals applications.
Biochem/physiol Actions
Inhibitor Type: Kinase
Protein Target: p38/SAPK2
Target Sub-Family: CMGC
Quality
Routinely evaluated in a kinase assay as an inhibitor.
Physical form
C20H14FN3O
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.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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
Thrombospondin stimulates focal adhesion disassembly through Gi- and phosphoinositide 3-kinase-dependent ERK activation
Orr, A. W., et al
The Journal of Biological Chemistry, 277, 20453-20460 (2002)
Katsushi Yamamoto et al.
The Journal of biological chemistry, 278(36), 34525-34532 (2003-06-25)
The accumulation of misfolded proteins in the endoplasmic reticulum (ER) evokes the ER stress response. The resultant outcomes are cytoprotective but also proapoptotic. ER chaperones and misfolded proteins exit to the secretory pathway and are retrieved to the ER, during
Z Li et al.
Biochemical and biophysical research communications, 228(2), 334-340 (1996-11-12)
We have identified a third member of the p38 group of MAP kinase termed p38 gamma. The cDNA for this MAP kinase encodes an 367 amino acid polypeptide that is slightly greater than 60% identical to p38 and p38 beta.
J C Lee et al.
Nature, 372(6508), 739-746 (1994-12-22)
Production of interleukin-1 and tumour necrosis factor from stimulated human monocytes is inhibited by a new series of pyridinyl-imidazole compounds. Using radiolabelled and radio-photoaffinity-labelled chemical probes, the target of these compounds was identified as a pair of closely related mitogen-activated
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