Insulysin, or insulin-degrading enzyme (IDE), is a zinc metallopeptidase of the inverzincin family. IDE is primarily located in the cytosol, but has been detected as a secreted enzyme and associated with the plasma membrane as well. The enzyme is expressed in many tissues, with the highest levels in liver, kidney, brain, and testis. IDE hydrolyzes a variety of regulatory peptides, including insulin, glucagon, atrial natriuretic factor, and transforming growth factor-a in vitro. In addition, IDE has been shown to degrade the amyloid b (Ab) peptide, which polymerizes into the plaques associated with Alzheimer’s disease. Deficiencies in IDE activity may contribute to the pathogenesis of type 2 diabetes mellitus (DM2) and Alzheimer’s disease. The IDE region of human chromosome 10q has been genetically linked to DM2. When the IDE gene was specifically disrupted in mice, IDE -/- animals developed hyperinsulinemia and glucose intolerance, characteristics of DM2. The IDE -/- mice were also shown to have a significant decrease in Ab degradation in the brain, resulting in increased cerebral accumulation of Ab peptide. This in vivo evidence is consistent with the hypotheses that IDE is important for the degradation of insulin in cells and for the clearance of Ab peptide in the brain. Rat Insulysin displays 95.5% and 98.5% sequence homology with human and mouse insulysin. ||Recombinant protein corresponding to Met42-Leu1019 from rat Insulysin fused to 5-His tag at N-terminal expressed in Spodoptera frugiperda, Sf 21. UniProt Accession: P35559.||Biological Activity:|Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPPGFSAFK(Dnp)-OH.||Specific Activity:|>1600pmol/min/ug||Storage and Stability:|Aliquot to avoid repeated freezing and thawing and store at -70°C. Stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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