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Serine/threonine-protein kinase/endoribonuclease IRE1 is a protein in humans that is encoded by ERN1 gene. Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation.
The following ERN1 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.
ERN1 Antibodies for Homo sapiens (Human)
| Code | Product Name | Species Reactivity | Application |
|---|---|---|---|
| CSB-PA007795LA01HU | ERN1 Antibody |
Human | ELISA, IHC |
| CSB-PA007795LB01HU | ERN1 Antibody, HRP conjugated |
Human | ELISA |
| CSB-PA007795LC01HU | ERN1 Antibody, FITC conjugated |
Human | |
| CSB-PA007795LD01HU | ERN1 Antibody, Biotin conjugated |
Human | ELISA |
| CSB-RA007795A724phHU | Phospho-ERN1 (S724) Recombinant Monoclonal Antibody |
Human | ELISA, WB, IF |
ERN1 Proteins for Homo sapiens (Human)
| Code | Product Name | Source |
|---|---|---|
| CSB-YP007795HU CSB-EP007795HU CSB-BP007795HU CSB-MP007795HU CSB-EP007795HU-B |
Recombinant Human Serine/threonine-protein kinase/endoribonuclease IRE1 (ERN1), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
ERN1 Proteins for Mus musculus (Mouse)
| Code | Product Name | Source |
|---|---|---|
| CSB-YP880635MO CSB-EP880635MO CSB-BP880635MO CSB-MP880635MO CSB-EP880635MO-B |
Recombinant Mouse Serine/threonine-protein kinase/endoribonuclease IRE1 (Ern1), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
Endoplasmic reticulum (ER) to nucleus signaling 1 protein, referred to as ERN1, is a human homologue of the yeast IRE1 ((inositol-requiring enzyme-1), so it is also called human IRE1α. ERN1 contains a cytoplasmic domain that is highly conserved to the yeast counterpart having a Ser/Thr protein kinase domain and a domain homologous to RNase L. ERN1/IRE1α is a special transmembrane sensor protein indispensable for the ER unfolded protein response (UPR). In unstressed cells, the ER luminal domain retains inactive as a monomer by binding to the ER chaperone HSPA5/BiP. Misfolded proteins build up in the ER, causing the release of HSPA5/BiP, which allows the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity. Activation of ERN1 by the association of its N-terminal ER luminal domains promotes autophosphorylation by its cytoplasmic kinase domain, leading to activation of the C-terminal ribonuclease domain, which splices Xbp1 mRNA generating an active Xbp1s transcriptional activator [1].
[1] Ali MM1, Bagratuni T, et al. Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response [J]. EMBO J. 2011 Mar 2;30(5):894-905.
