Analytical Data
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Gene name
IDE
- Application
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Alternative Names
Insulysin; Insulin Protease; Abeta-degrading protease; Insulinase
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
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Expression Region
Ala753~Pro973
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Molecular Weight
30kDa
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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
The study of IDE (Insulin-Degrading Enzyme) and its role as a protease has gained significant interest in the field of biochemistry and molecular biology. IDE is an intracellular enzyme primarily known for its ability to degrade insulin, thereby playing a crucial role in regulating insulin levels and glucose metabolism. Beyond insulin, IDE also degrades a variety of other peptides, including amyloid-beta, which is implicated in Alzheimer's disease. This multifunctionality positions IDE as a potential therapeutic target for metabolic disorders and neurodegenerative diseases. Research has flourished around the structural biology of IDE, elucidating its catalytic mechanisms and substrate specificity, which can inform the development of drugs aimed at modulating its activity. The reconstitution of IDE in vitro has allowed scientists to explore its dynamics and interactions with various substrates, enhancing our understanding of its physiological roles. Moreover, the pathological implications of IDE dysfunction have sparked investigations into how it may contribute to disease processes, particularly in the context of type 2 diabetes and cognitive decline. Overall, the reorganization and manipulation of IDE have promising implications for therapeutic advancements, highlighting the need for continued research in this vital area of study.
