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Sigma-Aldrich

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

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.

pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Acute Tox. 4 Oral

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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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)
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)
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.
A Cuenda et al.
FEBS letters, 364(2), 229-233 (1995-05-08)
A class of pyridinyl imidazoles inhibit the MAP kinase homologue, termed here reactivating kinase (RK) [Lee et al. (1994) Nature 372, 739-746]. We now show that one of these compounds (SB 203580) inhibits RK in vitro (IC50 = 0.6 microM)

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