IDE Human, Active
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
Greater than 90.0% as determined by SDS-PAGE.
Description
IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa.
IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Product Specs
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLISDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTAMSKLWF KQDDKFFLPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS
QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQGLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKLHH HHHH.
Product Science Overview
Insulin-Degrading Enzyme (IDE) is a zinc metallopeptidase that plays a crucial role in the regulation of insulin and other peptides. It is ubiquitously expressed in various tissues and is involved in the degradation of insulin, thereby terminating its activity. IDE is also implicated in the degradation of other peptides such as amyloid β-protein (Aβ), which is associated with Alzheimer’s disease .
IDE is a cytosolic proteinase with a molecular weight of approximately 110,000 Daltons. It shares structural and functional homology with bacterial protease III . The enzyme consists of two homologous halves, each contributing to the formation of a large catalytic cleft. This cleft allows IDE to selectively capture and degrade substrates based on size and charge complementarity .
The degradation process of insulin by IDE involves the enzyme binding to insulin and cleaving its peptide bonds without breaking the disulfide bonds . This selective degradation is facilitated by substrate-assisted catalysis, where the substrate itself stabilizes the disordered catalytic cleft of IDE .
The human recombinant form of IDE has been successfully expressed in various systems, including Chinese hamster ovary cells. This recombinant protein is indistinguishable from the native human enzyme in terms of size, immunoreactivity, and specific activity . The stable expression of recombinant IDE allows for functional studies and the development of potential therapeutic applications.
IDE dysfunction has been linked to several diseases, including type 2 diabetes mellitus and Alzheimer’s disease . By degrading insulin and amyloidogenic peptides, IDE plays a critical role in maintaining metabolic and neurological health. Understanding the molecular basis of IDE’s function and regulation can provide insights into developing IDE-based therapies for these conditions .
