Analytical Data
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Gene name
ERN2
- Application
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Alternative Names
IRE2
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Species
Human
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Source
Baculovirus
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Tag
N-His;N-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q76MJ5
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Expression Region
K499-R926
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Protein Length
Partial
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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
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Protein Description
ERN2 is an essential protein that has garnered significant attention in recent years due to its pivotal role in the endoplasmic reticulum (ER) stress response and the unfolded protein response (UPR). It is a member of the IRE1 family of transmembrane proteins, which are activated under conditions of ER stress, leading to the splicing of X-box binding protein 1 (XBP1) mRNA, a critical factor for cellular adaptation to stress. Dysregulation of ERN2 and the UPR has been implicated in various diseases, including neurodegenerative disorders, diabetes, and cancer, as cells respond inadequately to accumulating misfolded proteins. Research into ERN2 has revealed its dual function in promoting cell survival and apoptosis, depending on the severity and duration of stress. The ongoing study of ERN2 and its signaling pathways not only enhances our understanding of cellular stress mechanisms but also opens up potential therapeutic avenues for diseases linked to ER dysfunction. Given the rising incidence of disorders associated with protein misfolding, the exploration of ERN2-based interventions holds promise for modulating the UPR and improving cellular homeostasis under pathological conditions.
