PRODUCT NAME

IDE Polyclonal Antibody

CONJUGATION

Unconjugated

HOST

Mouse

SOURCE

KLH conjugated synthetic peptide derived from human IDE

IMMUNOGEN RANGE

491-590/1019

CLONALITY

Polyclonal

ISOTYPE

IgG

CONCENTRATION

1ug/ul

PURIFICATION

Purified by Protein A.

STORAGE BUFFER

Aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide.

STORAGE CONDITION

Store at -20°C for 12 months..

GENE ID

3416

SUBCELLULAR LOCATION

Cytoplasm, Cell membrane, Extracellular matrix

SYNONYMS

BC2; Insulin degrading enzyme; FLJ35968; insulin protease; insulinase; insulysin; Abeta-degrading protease; FLJ35968; Ide; IDE_HUMAN; Insulin-degrading enzyme; OTTHUMP00000020097.

BACKGROUND

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.

APPLICATION DILUTION

WB(1:300-1000), ELISA(1:500-1000), IHC-P(1:200-400), IHC-F(1:100-500)