Comparison

Insulin Degrading Enzyme (IDE) ELISA Kits Format 2 (human, mouse, rat, canine, rabbit)

Item no. IDE-ELISA
Manufacturer Fivephoton
Amount 1 kit, 96 T
Category
Type Elisa-Kit
Specific against Human (Homo sapiens), Mouse (Murine, Mus musculus), Rat (Rattus norvegicus), Dog (Canine, Canis lupus familiaris)
Citations Amata, O., Marino, T., Russo, N., & Toscano, M. (2009). Human insulin-degrading enzyme working mechanism. Journal of the American Chemical Society, 131(41), 14804-14811.

Bennett, R. G., Duckworth, W. C., & Hamel, F. G. (2000). Degradation of amylin by insulin-degrading enzyme. The Journal of Biological Chemistry, 275(47), 36621-36625.

Grasso, G., Rizzarelli, E., & Spoto, G. (2008). How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin.Biochimica et Biophysica Acta, 1784(7-8), 1122-1126.

Hong, M.-G., Reynolds, C., Gatz, M., Johansson, B., Palmer, J. C., Gu, H. F., Blennow, K., et al. (2008). Evidence that the gene encoding insulin degrading enzyme influences human lifespan. Human Molecular Genetics, 17(15), 2370-2378. Oxford University Press.

Im, H., Manolopoulou, M., Malito, E., Shen, Y., Zhao, J., Neant-Fery, M., Sun, C.-Y., et al. (2007). Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE. The Journal of Biological Chemistry, 282(35), 25453-25463.

Vepsalainen, S., Hiltunen, M., Helisalmi, S., Wang, J., Van Groen, T., Tanila, H., & Soininen, H. (2008). Increased expression of Abeta degrading enzyme IDE in the cortex of transgenic mice with Alzheimer’s disease-like neuropathology. Neuroscience Letters.
ECLASS 10.1 32160605
ECLASS 11.0 32160605
UNSPSC 41116126
Hazard information Sodium Azide (0.1%)
Available
Manufacturer - Targets
INS, IDE
Poisonous Material
Sodium Azide (0.1%)
Background
Insulin-degrading enzyme (abbreviated IDE), also known as insulysin or insulin protease, is a zinc-binding protease of the M16A metalloprotease subfamily known to cleave short polypeptides with variable sequences. IDE was first identified by its ability to degrade the B chain of insulin. IDE, which migrates at 110 kDa in gel electrophoresis under denaturing conditions, has since been shown to have additional substrates, including the signaling peptides glucagon, TGF alpha, beta-endorphin and amyloid-beta (Abeta).

In vitro and in vivo studies have shown correlations between IDE activity levels, Abeta degradation, and Alzheimer’s disease. Mice engineered to lack both alleles of the IDE gene exhibit a 50% decrease in Abeta degradation, resulting in cerebral accumulation of Abeta. Studies of genetically inherited forms of Alzheimer’s show reduction in both IDE expression and catalytic activity among affected individuals.
Highlights
Fully pre-configured sandwich ELISA format providing optimal convenience, specificity and sensitivity
Strip plate configuration allowing separate use and storage of 96-well ELISA plate sections
Affinity purified polyclonal or monoclonal capture antibodies coated on plate, depending on kit format. Separate HRP-conjugated detection antibody
Rapid colorimetric detection. 1 hr total incubation at 37C
Suitable for CSF, cell and tissue lysates and homogenates, other biological fluids
Highly sensitive: measures Insulin Degrading Enzyme concentration in pg/ml
Available for Human, rat, mouse, canine and rabbit Insulin Degrading Enzyme

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 1 kit, 96 T
Available: In stock
available

Compare

Add to wishlist

Get an offer

Request delivery time

Ask a technical question

Submit a bulk request

Questions about this Product?
 
Close