Insulin degrading enzyme / IDE peptide (Inactive domain) (ab41259)

Product Name 

Insulin degrading enzyme / IDE peptide (Inactive domain)

Product type 

Proteins and Peptides

Peptide 

This peptide was used as an immunogen for ab28561 - Insulin degrading enzyme / IDE antibody - Inactive domain.

Specificity 

We have a range of domain specific antibodies for this target. For a full list please see all Insulin degrading enzyme / IDE antibodies

Tested applications 
(see key)

ELISA, WB

Application notes 
(see key)

Recommended dilutions
ELISA: Use at an assay dependent dilution. WB: Use at an assay dependent dilution. This peptide can be used with studies using ab28561. Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.

Research areas 

Cell Biology >> Proteolysis / Ubiquitin >> Proteolytic enzymes >> Metalloprotease >> Insulysin
Neuroscience >> Neurology process >> Metabolism
Signal Transduction >> Growth Factors/Hormones >> Insulin / Insulin-like
Neuroscience >> Neurology process >> Neurodegenerative disease >> Alzheimer's disease >> Other

Relevance 

Insulysin was identified nearly a century ago as an enzyme responsible for the degradation of insulin in cells, although the precise interactions between insulin and insulysin remain elusive. Human insulysin was cloned in 1988, and shown to be a 118 kDa protein that exists primarily as a homodimer, and perhaps also complexed with other molecules. The sequence is well conserved between humans, rats and mice, and the antibody recognizes these species. Insulysin is a metalloproteinase of the clan ME, family M16, which contains an active site HxxEH, a reversal of the canonical HExxH zinc binding motif. Considered a zinc metalloproteinase, the activity of insulysin can be blocked with EDTA or 1-10 phenanthroline. In addition to the active metalloproteinase domain, insulysin contains a second metalloproteinase site which is considered catalytically inactive, and is thought to assist in substrate binding. Insulysin is most closely related to the bacterial proteinase pitrilysin, (the human orthologue of which appears to be MPRP1) and the mammalian proteinsae nardilysin. Generally thought to be a cytoplasmic protein, insulysin has been isolated from many different tissues and cell lines, and can degrade intact insulin, insulin B chain, glucagon, denatured hemoglobin, alpha amyloid protein, TGF alpha and amylin. Recent work implicates insulysin in clearing beta amyloid plaques from the brain, and has generated much interest in Alzheimer’s disease research. The pH optimum for insulysin is basic, pH 8.5, which also distinguishes it from other metalloproteinases.

Insulin degrading enzyme (IDE) has a preferential affinity for insulin such that the presence of insulin will inhibit IDE mediated degradation of other substrates. IDE degrades a variety of other peptides including atrial natriuretic peptide and amylin. IDE catabolizes A beta and has been implicated as a candidate enzyme responsible for the degradation and clearance of A beta in the brain. IDE has also been shown to degrade the APP intracellular domain (AICD), a product of gamma secretase cleaved APP that may function in nuclear signaling.

Purity 

>95% by SDS-PAGE

Storage buffer 

Preservative: None
Constituents: 0.001% Tween 20, 30mM HEPES, 2mM EDTA, 150mM Sodium chloride, pH 6.75

Form 

Liquid

Concentration 

1.000 mg/ml

Storage instructions 

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

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