Insulin degrading enzyme / IDE antibody [9B12.225] (ab25733)

Product Name 

Insulin degrading enzyme / IDE antibody [9B12.225]

Product type 

Primary antibodies

Description 

Mouse monoclonal [9B12.225] to Insulin degrading enzyme / IDE

Immunogen 

purified human erythrocyte IDE.

Reacts with 

Hu, Rat, Hm, Mk

Does not react with 
(species key)

Ms

Tested applications 
(see key)

IHC-P, IP, WB

Abreviews 

Customer reviews (see key)

Read about Abreviews

Application notes 
(see key)

Recommended dilutions
IHC-P: Use at an assay dependent dilution.
IP: 1/150.
WB: 1/1000. Detects a band of approximately ~110 kDa (predicted molecular weight: 110 kDa).

Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.

Cellular localization 

Cytoplasmic

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.

Database links 

Raised in 

Mouse

Clonality 

Monoclonal

Clone number 

9B12.225

Isotype 

IgG1

Light chain type 

kappa

Purity 

Ascites

Storage buffer 

Preservative: None
Constituents: Ascites

Form 

Liquid

Concentration 

1.000 mg/ml

Storage instructions 

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

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References for Insulin degrading enzyme / IDE antibody [9B12.225] (ab25733)

  This product has been used in: (two most recent references)

Du J et al. Metabolites of cerebellar neurons and hippocampal neurons play opposite roles in pathogenesis of Alzheimer's disease. PLoS One 4:e5530 (2009). WB. PubMed: 19436731

Bernstein HG et al. Regional and cellular distribution patterns of insulin-degrading enzyme in the adult human brain and pituitary. J Chem Neuroanat 35:216-24 (2008). PubMed: 18226493

See all 4 publication references for this product.


If you publish research using ab25733 please let us know so that we can cite the reference on this datasheet.

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