IRE1a (human) (rec.) (His) (active) (10µg)

IRE1α (Inositol-Requiring Enzyme 1 Alpha) is a bifunctional transmembrane protein kinase and endoribonuclease that serves as a central sensor of endoplasmic reticulum (ER) stress. As a key regulator of the unfolded protein response (UPR), IRE1α detects the accumulation of misfolded proteins in the ER lumen and initiates adaptive signaling pathways to restore proteostasis. Upon ER stress, IRE1α oligomerizes and undergoes autophosphorylation, activating its cytosolic RNase domain. This RNase activity catalyzes the unconventional splicing of XBP1 mRNA, producing a potent transcription factor that drives the expression of genes involved in protein folding, secretion, and ER-associated degradation (ERAD). In addition to XBP1 splicing, IRE1α mediates regulated IRE1-dependent decay (RIDD) of select mRNAs, linking ER stress to broader cellular signaling and fate decisions. IRE1α plays critical roles in cell survival, inflammation, metabolism, and apoptosis, and its dysregulation has been implicated in cancer, neurodegenerative diseases, diabetes, and inflammatory disorders. Due to its dual enzymatic activities and central position in UPR signaling, IRE1α is a widely studied target for investigations into ER stress mechanisms and for the development of small-molecule modulators. This IRE1α product is suitable for applications including biochemical assays, signaling pathway analysis, and studies of ER stress and unfolded protein response regulation.