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Recombinant Rat Insulin-degrading enzyme (Ide), partial

Recombinant Rat Insulin-degrading enzyme (Ide), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

Ide

Uniprot NO.

P35559

Alternative Names

Ide; Insulin-degrading enzyme; EC 3.4.24.56; Insulin protease; Insulinase; Insulysin

Species

Rattus norvegicus (Rat)

Source

Yeast

Expression Region

1-1019

Target Protein Sequence

MRNGLVWLLH PALPSTLHSI LGARPPPVKR LCGFPKQIYS TMNNPAIQRI EDHIVKSPED KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIPGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDASCKD REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVREE LLKFHSTYYS SNLMAICVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ LYKIVPIKDI RNLYVTFPIP DLQQYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGK LHYYPLNGVL TAEYLLEEFR PDLIDMVLDK LRPENVRVAI VSKSFEGKTD RTEQWYGTQY KQEAIPEDVI QKWQNADLNG KFKLPTKNEF IPTNFEILAL EKDATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKITEKMA TFEIDKKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG VMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ RRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKAIEDMTEE AFQKHIQALA IRRLDKPKKL SAECAKYWGE IISQQYNYDR DNIEVAYLKT LSKDDIIKFY KEMLAVDAPR RHKVSVHVLA REMDSCPVVG EFPSQNDINL SEAPPLPQPE VIHNMTEFKR GLPLFPLVKP HINFMAAKL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
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.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

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.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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

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
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
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
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
Proteolytically inactive insulin-degrading enzyme inhibits amyloid formation yielding non-neurotoxic abeta peptide aggregates. PMID:23593132
IDE-Met(1) links the mitochondrial biogenesis pathway with mitAbeta levels and organelle functionality. PMID:23525105
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
role played by somatostatin in preventing Abeta accumulation by partially restoring IDE activity PMID:22509294
a model in which the binding of anions activates insulin-degrading enzyme PMID:22049080
A region remote from the active site mediates allosteric activation of insulysin by peptides. PMID:21731629
These results demonstrate the sensitivity of insulin degradation by IDE to the redox environment. PMID:21448434
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
an insulin degrading enzyme (IDE) monomeric varint loses its regulatory properties PMID:20300529
Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD). PMID:11809755
a defect in Abeta proteolysis by IDE contributes to the accumulation of this peptide in the cortical microvasculature PMID:15489232
data suggest the presence of an allosteric regulatory site on insulysin that may shift its specificity toward small peptide substrates PMID:15494400
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
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
Insulysin was shown to initially cleave A(beta)1-40and A(beta)1-42 at His13-Gln14, His14-Gln15, and Phe19-Phe20 PMID:15800373
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
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