AG-CR1-0028-M0011 mgCHF 45.00
AG-CR1-0028-M0055 mgCHF 65.00
AG-CR1-0028-M02525 mgCHF 120.00
|Purity Chemicals||≥97% (HPLC)|
|Solubility||Soluble in methanol, DMSO or acetone; slightly soluble in ethyl acetate.|
|Identity||Determined by 1H-NMR.|
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
|Handling Advice||Protect from light.|
|Use/Stability||Stable for at least 2 years after receipt when stored at -20°C.|
|Product Specification Sheet|
- Potent and cell permeable p38 MAP kinase inhibitor [1, 2].
- Apoptosis inducer .
- Inhibits p38α and β, but not γ and δ isoforms [4, 5].
- Does not inhibit ERK2 or other members of the MAP kinase family or their upstream activators .
- JNK activator .
- Autophagic vacuole inducer 
- A protein kinase involved in the regulation of inflammatory cytokine biosynthesis: J.C. Lee, et al.; Nature 372, 739 (1994)
- SB202190, a selective inhibitor of p38 mitogen-activated protein kinase, is a powerful regulator of LPS-induced mRNAs in monocytes: C.L Manthey, et al.; J. Leukoc. Biol. 64, 409 (1998)
- Induction of apoptosis by SB202190 through inhibition of p38beta mitogen-activated protein kinase: S. Nemoto, et al.; J. Biol. Chem. 273, 16415 (1998)
- Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta): Y. Jiang, et al.; J. Biol. Chem. 271, 17920 (1996)
- The structural basis for the specificity of pyridinylimidazole inhibitors of p38 MAP kinase: K.P. Wilson, et al.; Chem. Biol. 4, 423 (1997)
- A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of p38 MAP kinase: T. Fox, et al.; Protein Sci. 7, 2249 (1998)
- Activation of c-Jun N-terminal kinase (JNK) by widely used specific p38 MAPK inhibitors SB202190 and SB203580: a MLK-3-MKK7-dependent mechanism: H. Muniyappa & K.C. Das; Cell. Signal. 20, 675 (2008)
- SB202190-induced cell type-specific vacuole formation and defective autophagy do not depend on p38 MAP kinase inhibition: MB. Menon, et al.; PLos One 6, e23054 (2011)
- A preliminary study on the proinflammatory mechanisms of Treponema pallidum outer membrane protein Tp92 in human macrophages and HMEC-1 cells: X. Luo, et al.; Microb. Pathog. 110, 176 (2017)