Key Specifications Table
|Uni Prot Number|
|Description||p38/SAPK2 Inhibitor (SB 202190)|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||3 years at -20°C|
|Material Size||1 mg|
|p38/SAPK2 (SB202190) - 2273150||2273150|
|p38/SAPK2 (SB202190) - DAM1655276||DAM1655276|
|p38/SAPK2 (SB202190) - DAM1724065||DAM1724065|
|p38/SAPK2 (SB202190) - DAM1739181||DAM1739181|
|p38/SAPK2 (SB202190) - DAM1769203||DAM1769203|
|p38/SAPK2 (SB202190) - DAM1776484||DAM1776484|
|p38/SAPK2 (SB202190) - DAM1787899||DAM1787899|
|p38/SAPK2 (SB202190) - JBC1864001||JBC1864001|
|Reference overview||Application||Pub Med ID|
|The KDEL Receptor Modulates the Endoplasmic Reticulum Stress Response through Mitogen-activated Protein Kinase Signaling Cascades|
Yamamoto, K., et al
J Biol Chem, 278:34525-32 (2003) 2003
|Thrombospondin stimulates focal adhesion disassembly through Gi- and phosphoinositide 3-kinase-dependent ERK activation|
Orr, A. W., et al
J Biol Chem, 277:20453-60 (2002) 2002
|p38 mitogen-activated protein kinase phosphorylates cytosolic phospholipase A2 (cPLA2) in thrombin-stimulated platelets. Evidence that proline-directed phosphorylation is not required for mobilization of arachidonic acid by cPLA2.|
Kramer, R M, et al.
J. Biol. Chem., 271: 27723-9 (1996) 1996
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 mitogen-activated protein kinase family (Kramer, R. M., Roberts, E. F., Strifler, B. A., and Johnstone, E. M. (1995) J. Biol. Chem. 270, 27395-27398) and also induces phosphorylation of cPLA2, thereby increasing its intrinsic catalytic activity. In the present study we have examined the role of p38 kinase in the phosphorylation and activation of cPLA2 in stimulated platelets. We have observed that activation of p38 kinase accompanies receptor-mediated events in platelets and coincides with cPLA2 phosphorylation. Furthermore, in the presence of inhibitors of p38 kinase, the proline-directed phosphorylation of cPLA2 was completely blocked in platelets stimulated with the thrombin receptor agonist peptide SFLLRN and was suppressed during the early (up to 2 min) phase of platelet stimulation caused by thrombin. Unexpectedly, we found that prevention of proline-directed phosphorylation of cPLA2 in stimulated platelets did not attenuate its ability to release arachidonic acid from platelet phospholipids. We conclude that: 1) cPLA2 is a physiological target of p38 kinase; 2) p38 kinase is involved in the early phosphorylation of cPLA2 in stimulated platelets; and 3) proline-directed phosphorylation of cPLA2 is not required for its receptor-mediated activation.
|The primary structure of p38 gamma: a new member of p38 group of MAP kinases.|
Li, Z, et al.
Biochem. Biophys. Res. Commun., 228: 334-40 (1996) 1996
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. Expression of its mRNA is primarily in muscle with no detectable expression in Northern blots using RNA from other tissues. In contrast to p38 and p38 beta, p38 gamma, fails to phosphorylate ATF-2 or MAPKAP kinase 2 but does like other MAP kinases phosphorylate MBP. In vivo kinase assays using protein extracts from skeletal muscle reveal that a 7-kDa protein is phosphorylated by p38 gamma but not by other members of this group of kinases. We suggest p38 gamma may have unique functions when compared with other members of the p38 group due to its restricted tissue expression and apparent substrate preferences.
|A protein kinase involved in the regulation of inflammatory cytokine biosynthesis.|
Lee, J C, et al.
Nature, 372: 739-46 (1994) 1994
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 protein kinase homologues, termed CSBPs. Binding of the pyridinyl-imidazole compounds inhibited CSBP kinase activity and could be directly correlated with their ability to inhibit cytokine production, suggesting that the CSBPs are critical for cytokine production.