Mouse Anti-IDE antibody | Sunlong Medical

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

Cat:

SL0018M

Species Reactivity：

Mouse,(predicted: Human,Rat,Chicken,Pig,Cow,)

Immunogen：

KLH conjugated synthetic peptide derived from human IDE:491-590/1019

Format：

Liquid

Storage instructions：

Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.

Concentration：

1mg/ml

Clonality：

Polyclonal

Isotype：

IgG

Applications：

WB=1:500-2000ELISA=1:5000-10000IHC-P=1:100-500IHC-F=1:100-500（Paraffin sections need to do antigen repair）not yet tested in other applications.optimal dilutions/concentrations should be determined by the end user.

Host：

Mouse

Product Overview：

Paraformaldehyde-fixed, paraffin embedded (mouse liver tissue); Antigen retrieval by boiling in sodium citrate buffer (pH6.0) for 15min; Block endogenous peroxidase by 3% hydrogen peroxide for 20 minutes; Blocking buffer (normal goat serum) at 37°C for 30min; Antibody incubation with (IDE) Polyclonal Antibody, Unconjugated (SL0018M) at 1:400 overnight at 4°C, followed by operating according to SP Kit(Rabbit) (sp-0023) instructionsand DAB staining.

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Unit:

Price: $228.00

Product PDFs

Datasheet: Down Datasheet

Other Information
Citations
Protein Attributes
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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.

Function:
Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.

Subunit:
Homodimer. Can form higher oligomers. Interacts (via N-terminus) with varicella-zoster virus (VZV) envelope glycoprotein E (via N-terminus); the membrane-associated isoform may function as an entry receptor for this virus.

Subcellular Location:
Cytoplasm. Cell surface. Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform.

Post-translational modifications:
The N-terminus is blocked.

Similarity:
Belongs to the peptidase M16 family.

SWISS:
P14735

Gene ID:
3416

Database links:

Entrez Gene: 3416 Human

Entrez Gene: 15925 Mouse

Entrez Gene: 25700 Rat

Omim: 146136 Human

SwissProt: P14735 Human

SwissProt: Q9JHR7 Mouse

SwissProt: P35559 Rat

Unigene: 500546 Human

Unigene: 28366 Mouse

Unigene: 45029 Rat

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