| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MME |
| 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 | 81.8kDa |
| 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MME重组蛋白的3篇参考文献示例(注：以下文献为虚构示例，仅用于格式参考)：
1. **《重组人MME蛋白在HEK293细胞中的表达及酶活性分析》**
作者：Zhang L, et al.
摘要：研究通过HEK293细胞系统成功表达具有活性的重组MME蛋白，并证实其可降解β-淀粉样蛋白，为阿尔茨海默病治疗提供潜在策略。
2. **《大肠杆菌表达系统中MME重组蛋白的优化纯化与结构表征》**
作者：Wang Y, et al.
摘要：优化了MME重组蛋白在大肠杆菌中的可溶性表达条件，通过亲和层析获得高纯度蛋白，并利用X射线晶体学解析其三维结构。
3. **《MME重组蛋白对心力衰竭模型动物的疗效研究》**
作者：Kimura T, et al.
摘要：在小鼠心力衰竭模型中验证了重组MME蛋白通过调节利钠肽代谢发挥心脏保护作用，提示其作为新型治疗分子的潜力。
MME (Membrane Metalloendopeptidase), also known as CD10 or neprilysin, is a zinc-dependent transmembrane enzyme belonging to the M13 family of endopeptidases. First identified in the 1970s, MME plays critical roles in regulating bioactive peptides by cleaving substrates such as enkephalins, natriuretic peptides, and amyloid-β. Its physiological functions span neural signaling modulation, blood pressure regulation, and immune response mediation through peptide degradation.
Recombinant MME proteins are engineered using expression systems (e.g., mammalian, insect, or bacterial cells) to produce purified, functional enzymes for research and therapeutic applications. These proteins retain the extracellular catalytic domain responsible for substrate hydrolysis while often excluding the transmembrane segment for solubility.
In biomedical research, recombinant MME is utilized to study peptide metabolism, neurodegenerative diseases (particularly Alzheimer's due to its amyloid-β degradation capacity), and cancer biology. Clinically, it serves as a diagnostic marker for certain leukemias and solid tumors. Therapeutic interest focuses on MME inhibitors (e.g., sacubitril in heart failure drugs) and its potential in targeting tumor microenvironments. Recent studies also explore its role in pain management through opioid peptide regulation and in mitigating protein aggregation pathologies.
The production of recombinant MME enables structure-function analyses, drug screening, and biotechnological applications requiring controlled peptide processing, making it a versatile tool in both basic science and pharmaceutical development.
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