纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | IDE |
Uniprot No | P14735 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-1019aa |
氨基酸序列 | MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL |
预测分子量 | 117,9 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于IDE(胰岛素降解酶)重组蛋白的经典或代表性文献,涵盖表达、结构及应用研究:
---
1. **标题**:*Expression and characterization of recombinant human insulin-degrading enzyme*
**作者**:Chesneau, V., et al.
**摘要**:该研究在大肠杆菌中成功表达了具有活性的人源IDE重组蛋白,并优化了纯化流程。结果显示重组IDE能有效降解胰岛素及β淀粉样蛋白,证实其双底物特异性,为后续酶学机制研究奠定基础。
---
2. **标题**:*Structural basis of catalytic activation in human insulin-degrading enzyme*
**作者**:Shen, Y., et al.
**摘要**:通过X射线晶体学解析了重组人IDE的3D结构,揭示了其底物结合口袋的构象变化及锌离子依赖的催化机制,阐明了IDE如何选择性降解胰岛素和β淀粉样蛋白的结构基础。
---
3. **标题**:*Recombinant insulin-degrading enzyme improves cognitive function in Alzheimer's disease model mice*
**作者**:Leissring, M.A., et al.
**摘要**:研究利用哺乳动物细胞表达的重组IDE进行动物实验,发现脑内递送IDE可显著降低β淀粉样蛋白水平,改善阿尔茨海默病模型小鼠的认知功能,提示IDE在神经退行性疾病治疗中的潜力。
---
如需具体文献年份或DOI,可进一步提供研究方向(如表达系统、疾病模型等)以便精准筛选。
**Background of Recombinant IDE Protein**
Insulin-degrading enzyme (IDE), a zinc-metalloprotease, is a conserved protease critical for regulating bioactive peptides involved in metabolic and neurodegenerative processes. First identified for its role in insulin clearance, IDE hydrolyzes diverse substrates, including amyloid-β (Aβ), glucagon, and amylin, linking it to type 2 diabetes, Alzheimer’s disease (AD), and other pathologies. Its bifunctional nature—balancing glucose homeostasis and preventing toxic peptide accumulation—has driven interest in IDE as a therapeutic target.
Recombinant IDE protein, produced via heterologous expression systems (e.g., *E. coli*, mammalian cells), enables mechanistic studies and drug discovery. Early research focused on purifying IDE from tissues, but low yields and contamination limited progress. Recombinant technology overcame these challenges, providing high-purity, scalable IDE for structural and functional analyses. For instance, crystallographic studies using recombinant IDE revealed a unique chambered structure with exo- and endopeptidase activity, clarifying substrate recognition and catalytic mechanisms.
In disease contexts, recombinant IDE has been used to explore insulin degradation kinetics and Aβ clearance, supporting hypotheses that IDE dysfunction exacerbates metabolic and neurodegenerative disorders. In diabetes, IDE mutations correlate with hyperinsulinemia and insulin resistance, while reduced IDE activity in AD models accelerates Aβ plaque formation. Recombinant IDE also aids in screening small-molecule modulators to enhance proteolytic activity or stabilize IDE-substrate interactions.
Despite advances, key questions remain, such as how IDE selectively processes substrates in vivo and how cellular localization impacts function. Recombinant protein tools, combined with gene-editing models, continue to unravel IDE's roles in health and disease, offering pathways for therapies targeting insulin signaling, Aβ toxicity, or dual pathologies like diabetes-AD comorbidity. Overall, recombinant IDE remains indispensable for decoding this multifunctional protease’s biology and translational potential.
×