Recombinant Rat Insulin-degrading enzyme (Ide), partial

Code CSB-YP010988RA
MSDS
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Source Yeast
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Code CSB-EP010988RA
MSDS
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Source E.coli
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Code CSB-EP010988RA-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP010988RA
MSDS
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Source Baculovirus
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Code CSB-MP010988RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Ide
Uniprot No.
Alternative Names
Ide; Insulin-degrading enzyme; EC 3.4.24.56; Insulin protease; Insulinase; Insulysin
Species
Rattus norvegicus (Rat)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

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. Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin. 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. Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia. Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP. Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients. 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.
Gene References into Functions
  1. data suggest that insulin deprivation, rather than high glucose, is a significant determinant of IDE regulation; as evidence indicates potential roles for IDE in diabetes and Alzheimer's disease, understanding the mechanisms regulating IDE expression may be important in developing new treatment strategies PMID: 29940507
  2. This study concluded that vitamin D3 ameliorated insulin resistance and hyperinsulinemia in diabetic rat model received high fructose water through reduction of insulin-degrading enzyme and activation of insulin receptor phosphorylation. PMID: 27930980
  3. Ageing and diabetes are accompanied by a deficit of IDE in the brain structures where accumulation of Abeta was reported in Azheimer disease patients. PMID: 25792373
  4. Insulin-degrading enzyme is able to degrade specific amino acid sequences present in the neuropeptide pro-NPFFA (NPFF precursor), generating some cryptic peptides that are also observed after incubation with rat brain cortex homogenate. PMID: 25247577
  5. Proteolytically inactive insulin-degrading enzyme inhibits amyloid formation yielding non-neurotoxic abeta peptide aggregates. PMID: 23593132
  6. IDE-Met(1) links the mitochondrial biogenesis pathway with mitAbeta levels and organelle functionality. PMID: 23525105
  7. Mutation of each cysteine residue individually revealed cysteine 904 as the key residue required for maximal activity and polyanion activation, although other cysteines affect polyanion binding to a lesser extent. PMID: 23077523
  8. role played by somatostatin in preventing Abeta accumulation by partially restoring IDE activity PMID: 22509294
  9. a model in which the binding of anions activates insulin-degrading enzyme PMID: 22049080
  10. A region remote from the active site mediates allosteric activation of insulysin by peptides. PMID: 21731629
  11. These results demonstrate the sensitivity of insulin degradation by IDE to the redox environment. PMID: 21448434
  12. The three Abeta-degrading enzymes were damaged to different extents in the brain of diabetic rats, and impairment of ECE-1 and IDE partly contributed to the elevated Abeta(1-40) levels in brain of diabetic rats. PMID: 20414044
  13. an insulin degrading enzyme (IDE) monomeric varint loses its regulatory properties PMID: 20300529
  14. Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD). PMID: 11809755
  15. a defect in Abeta proteolysis by IDE contributes to the accumulation of this peptide in the cortical microvasculature PMID: 15489232
  16. data suggest the presence of an allosteric regulatory site on insulysin that may shift its specificity toward small peptide substrates PMID: 15494400
  17. To test the hypothesis that insulin might upregulate IDE via a negative feedback control mechanism, we used both in vitro and in vivo strategies to determine the impact of insulin signaling on IDE levels. PMID: 15590928
  18. Active site mutations of insulin-degrading enzyme are suggested not only to reduce catalytic activity but also cause local conformational changes that affect the allosteric properties of the enzyme. PMID: 15749695
  19. Insulysin was shown to initially cleave A(beta)1-40and A(beta)1-42 at His13-Gln14, His14-Gln15, and Phe19-Phe20 PMID: 15800373
  20. IDE participates in prostatic and uterine growth;testosterone or estradiol are important for the expression and regulation of IDE in the prostate and uterus. PMID: 15985623
  21. study the role that ubiquitin plays on IDE capability of binding and degrading insulin molecules and the obtained results indicate that ubiquitin has an allosteric role for IDE and high ubiquitin levels impair IDE activity PMID: 18489915

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Subcellular Location
Cytoplasm, cytosol. Cell membrane. Secreted.
Protein Families
Peptidase M16 family
Tissue Specificity
Detected in brain (at protein level).
Database Links
CUSABIO guaranteed quality
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