This gene encodes a zinc metallopeptidase that degrades intracellular insulin, and thereby terminates insulins activity, as well as participating in intercellular peptide signalling by degrading diverse peptides such as glucagon, amylin, bradykinin, and kallidin. The preferential affinity of this enzyme for insulin results in insulin-mediated inhibition of the degradation of other peptides such as beta-amyloid. Deficiencies in this protein's function are associated with Alzheimer's disease and type 2 diabetes mellitus but mutations in this gene have not been shown to be causitive for these diseases. This protein localizes primarily to the cytoplasm but in some cell types localizes to the extracellular space, cell membrane, peroxisome, and mitochondrion. Alternative splicing results in multiple transcript variants encoding distinct isoforms. Additional transcript variants have been described but have not been experimentally verified.[provided by RefSeq, Sep 2009].
custom-made
IDE
Spezies: Maus
Wirt: HEK-293 Cells
Recombinant
> 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
custom-made
IDE
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
> 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
custom-made
IDE
Spezies: Maus
Wirt: Cell-free protein synthesis (CFPS)
Recombinant
approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
WB, SDS, ELISA
custom-made
IDE
Spezies: Human
Wirt: Cell-free protein synthesis (CFPS)
Recombinant
approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
WB, SDS, ELISA
Kim, Lone, Saghatelian: "Analysis of the proteolysis of bioactive peptides using a peptidomics approach." in: Nature protocols, Vol. 8, Issue 9, pp. 1730-42, (2013) (PubMed).