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Merck
CN
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文件

19-135

Sigma-Aldrich

p38/SAPK2 抑制剂(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代码:
12352200
eCl@ss:
32160405
NACRES:
NA.41

质量水平

形式

solid

制造商/商品名称

Upstate®

技术

activity assay: suitable (kinase)

NCBI登记号

UniProt登记号

运输

wet ice

应用

p38/SAPK2的高特异性抑制剂

生化/生理作用

抑制剂种类:激酶
蛋白质靶标:p38/SAPK2
靶标亚家族:CMGC

质量

通过激酶测定法进行常规评估。

外形

C12H16FN3OS

储存及稳定性

在-20°C下可保存3年

法律信息

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

免责声明

除非我们的产品目录或产品附带的其他公司文档另有说明,否则我们的产品仅供研究使用,不得用于任何其他目的,包括但不限于未经授权的商业用途、体外诊断用途、离体或体内治疗用途或任何类型的消费或应用于人类或动物。

象形图

Exclamation mark

警示用语:

Warning

危险声明

危险分类

Acute Tox. 4 Oral

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


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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
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)
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.

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