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APY29 inhibited IRE1α autophosphorylation (IC50 = 280 nM) and activated IRE1α ribonucase activity. Even in the absence of upstream ER stress, APY29 occupies the kinase ATP-binding site of IRE1α and activates RNASE-mediated SPLicting of XBP1 mRNA. In vitro inhibition of IRE1α kinase autophosphorylation by IC50 ~0.28 μM was dose-dependent. Since abnormal regulation of UPR is associated with a variety of cellular degeneration and tumor diseases, small molecule modulators of IRE1α, such as APY29, could serve as useful tools for understanding the role of UPR in pathophysiology and for developing endoplasmic reticulum stress-related disease compounds.
| Molecular Weight | 332.36 |
| Formula | C17H16N8 |
| CAS Number | 1216665-49-4 |
| Solubility (25°C) | DMSO |
| Storage |
Powder -20°C 3 years ; 4°C 2 years In solvent -80°C 6 months ; -20°C 1 month |
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