| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NEP |
| Uniprot No | P08473 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 52-750aa |
| 氨基酸序列 | YDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW |
| 预测分子量 | 81.8 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. |
以下是关于NEP(Neprilysin)重组蛋白研究的示例参考文献(注：以下为模拟示例，非真实文献，仅供格式参考)：
1. **文献名称**："High-yield expression and purification of recombinant human neprilysin in Escherichia coli"
**作者**：Smith J, et al.
**摘要**：研究报道了通过大肠杆菌表达系统高效表达重组人NEP蛋白的优化方法，分析了纯化工艺及酶活鉴定，证实其具有降解β-淀粉样蛋白的功能。
2. **文献名称**："Functional characterization of a novel recombinant neprilysin variant for therapeutic applications"
**作者**：Li X, Wang Y.
**摘要**：通过基因工程技术构建了具有增强稳定性的NEP突变体，验证其在体外模型中对血管紧张肽的降解效率，为心血管疾病治疗提供潜在候选分子。
3. **文献名称**："Structural insights into recombinant neprilysin by cryo-EM and molecular dynamics simulations"
**作者**：Garcia R, et al.
**摘要**：利用冷冻电镜和分子动力学模拟解析了重组NEP的三维结构，揭示了其底物结合域的关键氨基酸残基，为理性设计功能改良酶提供理论依据。
4. **文献名称**："Recombinant neprilysin delivery via nanoparticles ameliorates cognitive deficits in Alzheimer's disease mice"
**作者**：Chen H, et al.
**摘要**：开发了纳米颗粒包裹的重组NEP递送系统，证明其能有效穿越血脑屏障并减少阿尔茨海默病模型小鼠脑内的β-淀粉样蛋白沉积。
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如需真实文献，建议通过PubMed或Web of Science检索关键词“recombinant neprilysin”或“NEP protein expression”获取近年研究。
**Background of NEP Recombinant Protein**
NEP (Neprilysin), also known as membrane metallo-endopeptidase or CD10. is a zinc-dependent metalloprotease widely recognized for its role in regulating bioactive peptides. Initially discovered in the 1970s, NEP cleaves peptide bonds at hydrophobic residues, influencing physiological processes such as blood pressure regulation, pain modulation, and immune response. It targets substrates including atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP), endothelin-1. and enkephalins, thereby modulating their biological activity.
Therapeutic interest in NEP surged with the development of sacubitril/valsartan (Entresto®), a dual-acting angiotensin receptor-neprilysin inhibitor approved for heart failure. By inhibiting NEP, this drug potentiates natriuretic peptides, promoting vasodilation and sodium excretion. Recombinant NEP proteins, produced via bacterial or mammalian expression systems, are critical tools for studying enzymatic mechanisms, screening inhibitors, and understanding disease pathways.
Structurally, recombinant NEP retains the extracellular catalytic domain (∼700 amino acids) responsible for proteolytic activity. Its applications span cardiovascular research, neurodegeneration (e.g., amyloid-β degradation), and cancer (NEP is downregulated in some malignancies). However, challenges remain in optimizing stability and activity for therapeutic use. Continued research on NEP recombinant proteins aims to refine drug design and explore novel therapeutic targets, reinforcing its significance in both basic science and clinical innovation.
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