Analytical Data
-
Gene name
Insulysin/IDE
- Application
-
Alternative Names
Insulysin; Insulin Protease; Abeta-degrading protease; Insulinase
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P14735
-
Expression Region
Ala753~Pro973
-
Molecular Weight
30kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Insulysin, also known as insulin-degrading enzyme (IDE), is a zinc-dependent metalloprotease primarily involved in the degradation of insulin and other peptide hormones. Its role in glucose homeostasis and insulin sensitivity has made it a critical target for research related to diabetes and metabolic disorders. Over the years, studies have shown that IDE not only regulates insulin levels but may also modulate the clearance of amyloid-beta peptides, implicating it in neurodegenerative diseases like Alzheimer’s. The ability of IDE to degrade multiple substrates underscores its significance in various physiological processes. The development of recombinant IDE proteins has advanced our understanding of its structure, function, and regulatory mechanisms, allowing researchers to study its activity and inhibition in more detail. Such studies are vital for exploring therapeutic strategies aimed at manipulating IDE activity to improve insulin sensitivity or reduce amyloid accumulation in the brain. As a result, IDE is emerging as a promising target for novel treatments for both metabolic syndromes and neurodegenerative diseases, highlighting the need for further investigation into its enzymatic properties and potential as a biomarker.
