Recombinant mouse IRE1 protein (Active)
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Recombinant mouse IRE1 protein (Active) is a Mouse Fragment protein, in the 469 to 977 aa range, expressed in Baculovirus infected Sf9 cells, with >90%, suitable for SDS-PAGE, FuncS.
View Alternative Names
Ire1, Ern1, Serine/threonine-protein kinase/endoribonuclease IRE1, Endoplasmic reticulum-to-nucleus signaling 1, Inositol-requiring protein 1, Ire1-alpha, IRE1a
- FuncS
Supplier Data
Functional Studies - Recombinant mouse IRE1 protein (Active) (AB268540)
The specific acivity of ab268540 was 34 nmol/min/mg in a kinase assay using myelin basic protein as substrate.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant mouse IRE1 protein (Active) (AB268540)
SDS-PAGE analysis of ab268540.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
IRE1 is an important regulator in the unfolded protein response (UPR) a cellular reaction to stress in the ER. It operates as part of a complex mechanism facilitating the splicing of X-box binding protein 1 (XBP1) mRNA which results in the production of a potent transcription factor. IRE1 activity helps in restoring normal function of the cell by upregulating genes involved in protein folding secretion and degradation. Its actions are important for maintaining cellular homeostasis during stressful conditions.
Pathways
IRE1 is an integral component of the UPR pathway which works to alleviate ER stress. It interacts closely with other UPR transducers such as activating transcription factor 6 (ATF6) and protein kinase RNA-like ER kinase (PERK). IRE1 connects with the XBP1 pathway facilitating adaptive responses that enhance protein-folding capacity lipid biosynthesis and ER-associated degradation. Altogether these pathways mediate cell survival or apoptosis depending on the severity of the stress.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed : 11850408, PubMed : 25164867). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. 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 : 25164867). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed : 11850408, PubMed : 25164867). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed : 11850408, PubMed : 25164867). Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A (By similarity).
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Post-translational modifications
Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain (PubMed:25164867). In response to ER stress, phosphorylated at Ser-724, Ser-729 and possibly Ser-726; phosphorylation promotes oligomerization and endoribonuclease activity (PubMed:30118681). Dephosphorylated at Ser-724, Ser-729 and possibly Ser-726 by RPAP2 to abort failed ER-stress adaptation and trigger apoptosis (By similarity).. ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities.
Target data
Product promise
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