Recombinant Human Insulin degrading enzyme / IDE protein (His tag N-Terminus)
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Recombinant Human Insulin degrading enzyme / IDE protein (His tag N-Terminus) is a Human Fragment protein, in the 42 to 1019 aa range, expressed in Baculovirus infected Sf9 cells, with >80%, suitable for SDS-PAGE.
View Alternative Names
Insulin-degrading enzyme, Abeta-degrading protease, Insulin protease, Insulysin, Insulinase, IDE
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Insulin degrading enzyme / IDE protein (His tag N-Terminus) (AB271547)
SDS-PAGE analysis of ab271547.
Complementary Products
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
IDE manages the levels of insulin and other peptides by degrading them preventing accumulation and maintaining homeostasis. It is not part of a complex but it acts individually in cellular environments to modulate the concentration of its substrates. IDE is important for controlling insulin availability and turnover which impacts glucose metabolism. By influencing the degradation of insulin IDE aids in balancing metabolic demands with insulin availability.
Pathways
IDE plays a vital role in insulin signaling and glucose metabolic processes. It is directly involved in the insulin signaling pathway by regulating insulin levels which consequently affects cellular responses to insulin. IDE connects with several proteins associated with these pathways including insulin receptor and glucose transporters ensuring proper cell signaling and metabolic functions. By modulating insulin levels IDE helps optimize glucose uptake and storage.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling (PubMed : 10684867, PubMed : 17051221, PubMed : 17613531, PubMed : 18986166, PubMed : 19321446, PubMed : 21098034, PubMed : 2293021, PubMed : 23922390, PubMed : 24847884, PubMed : 26394692, PubMed : 26968463, PubMed : 29596046). Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (PubMed : 23922390, PubMed : 26394692, PubMed : 29596046). Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP (By similarity). Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia (Probable) (PubMed : 26394692, PubMed : 9830016). Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP (PubMed : 21098034). Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients (PubMed : 21098034). Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I.. (Microbial infection) The membrane-associated isoform acts as an entry receptor for varicella-zoster virus (VZV).
Sequence similarities
Belongs to the peptidase M16 family.
Post-translational modifications
The N-terminus is blocked.
Target data
Product promise
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