IRE1 Protein, Human (sf9, His-GST)

IRE1 is a key serine/threonine protein kinase and endoribonuclease essential for sensing the unfolded protein response (UPR) in the endoplasmic reticulum. In cellular homeostasis, it remains monomeric by binding to HSPA5/BiP. IRE1 Protein, Human (sf9, His-GST) is the recombinant human-derived IRE1 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of IRE1 Protein, Human (sf9, His-GST) is 513 a.a., with molecular weight of ~90 kDa.

IRE1, a serine/threonine-protein kinase and endoribonuclease, serves as a pivotal sensor in the endoplasmic reticulum unfolded protein response (UPR). In the absence of cellular stress, the endoplasmic reticulum luminal domain maintains its inactive monomeric state through binding to the endoplasmic reticulum chaperone HSPA5/BiP. Upon the accumulation of misfolded proteins, the release of HSPA5/BiP allows the luminal domain to homodimerize, facilitating autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity. This endoribonuclease activity is specific to XBP1 mRNA, excising 26 nucleotides from the XBP1 transcript. The resulting spliced XBP1 transcript encodes a transcriptional activator that up-regulates the expression of UPR target genes. Beyond its role in the UPR, IRE1 acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional trafficking of CFTR to the cell membrane by modulating the expression and localization of SEC16A, highlighting its involvement in diverse cellular processes beyond the UPR.

Human

Sf9 insect cells

N-His;N-GST

O75460 (P465-L977)

2081  [NCBI]

Approximately 90 kDa

Greater than 80% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.