IRE
Inositol-requiring enzyme 1 (IRE1; EC 2.7.11.1) is an endoplasmatic reticulum (ER) transmembrane sensor that activates the unfolded protein response (UPR) through a cytoplasmic kinase domain and an RNase domain to maintain the ER and cellular function[1]. On ER stress, IRE1 RNase is activated through conformational change, autophosphorylation, and higher-order oligomerization. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis[2].
[1] IRE1: ER stress sensor and cell fate executor. Y. Chen, F. Brandizzi. Trends Cell Biol. 2013, pii, S0962-8924.
[2] A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. W. Tirasophon, A.A. Welihinda, R.J. Kaufman. Genes Dev. 1998, 12, 1812-1824.
| Axon ID | Name | Description | From price | |
|---|---|---|---|---|
| 1902 | 4μ8C | IRE1α inhibitor | €105.00 | |
| 1656 | Irestatin 9389 | IRE1 inhibitor; UPR inhibitor | €125.00 | |
| 4087 | IXA4 | Highly selective IRE1/XBP1s activator | €120.00 | |
| 3670 | MKC-3946 | Potent and selective IRE1α inhibitor | €120.00 | |
| 3223 | MKC8866 | Potent IRE1α inhibitor | €105.00 | |
| 1670 | STF 083010 | IRE1α inhibitor | €95.00 | |