| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | E & M |
| Uniprot No | P03519 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-229aa |
| 氨基酸序列 | MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTYDPNQLRYEKFFFTVKMTVRSNRPFRTYSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHTHCEGRAYLPHRMGKTPPMLNVPEHFRRPFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWVLDSISHFK |
| 预测分子量 | 26,0 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E蛋白(Envelope)和M蛋白(Matrix/Membrane)重组蛋白的3篇文献示例，涵盖病毒结构、疫苗开发及重组表达技术：
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1. **文献名称**: *Structural and functional analysis of the Ebola virus glycoprotein and matrix protein interactions*
**作者**: Lee, J.E., et al.
**摘要**: 本研究解析了埃博拉病毒E蛋白(GP)与M蛋白(VP40)的相互作用机制，通过重组表达技术获得两种蛋白的复合物结构。实验表明，M蛋白通过调控E蛋白的构象变化促进病毒组装，为抗病毒药物设计提供了新靶点。
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2. **文献名称**: *Recombinant co-expression of SARS-CoV-2 M and E proteins in mammalian cells generates virus-like particles as vaccine candidates*
**作者**: Zhang, L., et al.
**摘要**: 研究利用哺乳动物细胞共表达新冠病毒M和E重组蛋白，成功自组装成病毒样颗粒(VLPs)。动物实验显示，该VLPs可诱导中和抗体，证明其作为新冠亚单位疫苗的潜力。
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3. **文献名称**: *Expression and purification of functional MERS-CoV envelope and membrane proteins in a bacterial system*
**作者**: Alharbi, N.K., et al.
**摘要**: 开发了一种基于大肠杆菌的重组表达系统，高效纯化MERS冠状病毒的E和M蛋白。通过体外复性实验证实两种蛋白具有天然构象，为快速制备诊断抗原奠定基础。
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**备注**：若需特定病毒(如HIV、流感病毒等)或应用领域(如癌症治疗)的相关文献，可进一步补充说明。以上文献为虚构示例，实际引用需查询PubMed/Google Scholar等数据库。
Recombinant E and M proteins are critical components in virology and biomedical research, particularly in studying enveloped viruses like coronaviruses. The envelope (E) protein, a small integral membrane protein, and the membrane (M) protein, a transmembrane glycoprotein, play essential roles in viral assembly, budding, and pathogenesis. The E protein facilitates virion morphogenesis and membrane curvature, while the M protein acts as a central organizer of viral structure, interacting with the nucleocapsid and spike proteins to stabilize the viral envelope. Their structural and functional significance has driven interest in producing recombinant versions for research and therapeutic applications.
Recombinant protein technology enables large-scale production of E and M proteins using heterologous expression systems such as *E. coli*, yeast, or mammalian cell cultures. These systems allow precise control over protein folding, post-translational modifications, and purification. For instance, mammalian systems like HEK293 or CHO cells are preferred for producing glycosylated M proteins that mimic native conformations. Recombinant E and M proteins are instrumental in structural studies (e.g., cryo-EM, X-ray crystallography), antiviral drug screening, and serological assay development. During the COVID-19 pandemic, they were used to study SARS-CoV-2 entry mechanisms and evaluate neutralizing antibodies.
Challenges include maintaining protein stability due to their hydrophobic nature and ensuring proper membrane integration. Advanced strategies like fusion tags, lipid nanodiscs, or virus-like particles (VLPs) are employed to enhance solubility and functionality. Additionally, recombinant E and M proteins serve as antigen candidates for subunit vaccines, offering safer alternatives to live-attenuated viruses. Their ability to elicit immune responses without viral replication makes them attractive for next-generation vaccine design. Ongoing research focuses on optimizing expression platforms and leveraging these proteins for broad-spectrum antiviral therapies, underscoring their continued relevance in combating emerging infectious diseases.
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