Anti-IRE1p antibody (3655) was raised against a peptide corresponding to 16 amino acids near the carboxy terminus of human IRE1P. The immunogen is located within the last 50 amino acids of IRE1p.
Conjugation:
Unconjugated
Alternative Names:
Endoplasmic reticulum-to-nucleus signaling 1,ER to nucleus signalling 1,hIRE1p,inositol-requiring 1,inositol-requiring enzyme 1,inositol-requiring protein 1,IRE1,IRE1a,ire1-alpha,IRE1P,protein kinase/endoribonuclease,serine/threonine-protein kinase/endoribonuclease IRE1.
Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11779464, PubMed:11175748, PubMed:12637535, PubMed:9637683, PubMed:21317875). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP (PubMed:21317875). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity (PubMed:21317875). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11779464, PubMed:24508390, PubMed:21317875). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11779464, PubMed:24508390, PubMed:21317875).
