Analytical Data
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Gene name
IRE1
- Application
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Alternative Names
IRE1; IRE1P; Serine/Threonine-Protein Kinase/Endoribonuclease IRE1; Inositol-requiring protein 1; Ire1-alpha; Serine/threonine-protein kinase; Endoribonuclease
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
O75460
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Expression Region
Phe571~Phe832
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Molecular Weight
36kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
IRE1 (Inositol-requiring enzyme 1) is a critical component of the unfolded protein response (UPR), a cellular stress response activated by the accumulation of misfolded proteins in the endoplasmic reticulum (ER). Research on IRE1 has gained significant attention due to its dual role as a sensor of ER stress and as an endoribonuclease that regulates the splicing of X-box binding protein 1 (XBP1), ultimately influencing cell survival and apoptosis. Dysregulation of IRE1 activity is implicated in various diseases, including neurodegenerative disorders, diabetes, and cancer, making it a potential therapeutic target. Recent studies have explored the structural and functional aspects of IRE1, revealing its complex regulation and the potential for pharmacological modulation. Additionally, the development of recombinant IRE1 proteins has facilitated the investigation of its mechanisms at a molecular level, enhancing our understanding of how it contributes to cellular homeostasis under stress conditions. As research progresses, the therapeutic implications of modulating IRE1 activity in disease contexts are becoming increasingly salient.
