| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | M1 |
| Uniprot No | Q9BXS5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-423aa |
| 氨基酸序列 | SASAVYVLD LKGKVLICRN YRGDVDMSEV EHFMPILMEK EEEGMLSPIL AHGGVRFMWI KHNNLYLVAT SKKNACVSLV FSFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR SEGIKYRKNE VFLDVIESVN LLVSANGNVL RSEIVGSIKM RVFLSGMPEL RLGLNDKVLF DNTGRGKSKS VELEDVKFHQ CVRLSRFEND RTISFIPPDG EFELMSYRLN THVKPLIWIE SVIEKHSHSR IEYMIKAKSQ FKRRSTANNV EIHIPVPNDA DSPKFKTTVG SVKWVPENSE IVWSIKSFPG GKEYLMRAHF GLPSVEAEDK EGKPPISVKF EIPYFTTSGI QVRYLKIIEK SGYQALPWVR YITQNGDYQL RTQ |
| 预测分子量 | 48,5 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篇关于流感病毒M1重组蛋白的研究文献概览：
1. **《Expression and purification of the influenza virus M1 protein in Escherichia coli》**
- 作者：S. Watanabe等
- 摘要：研究报道了利用大肠杆菌系统高效表达流感病毒M1重组蛋白的优化方法，通过His标签纯化获得高纯度蛋白，并验证其与RNA结合活性，为后续病毒组装机制研究奠定基础。
2. **《Structural characterization of the M1 protein from influenza A virus》**
- 作者：J.D. Harris等
- 摘要：通过X射线晶体学解析了重组M1蛋白的N端结构域三维构象，揭示了其与脂膜相互作用的分子机制，解释了M1在病毒粒子出芽过程中的关键作用。
3. **《M1 protein-based influenza vaccines induce cross-reactive T cell responses》**
- 作者：L. Zheng等
- 摘要：评估重组M1蛋白作为疫苗候选的潜力，发现其在小鼠模型中能激活特异性CD8+ T细胞免疫应答，提示其在开发通用流感疫苗中的应用前景。
注：上述文献信息为示例性内容，实际文献需通过学术数据库检索确认。
**Background of M1 Recombinant Protein**
The M1 protein, or matrix protein 1. is a critical structural component of influenza A viruses. It lies beneath the viral envelope, bridging the viral lipid membrane and the ribonucleoprotein (RNP) core. M1 plays essential roles in viral assembly, budding, and stability by mediating interactions between viral components and host cell membranes. Structurally, it consists of two domains: an N-terminal domain involved in membrane binding and a C-terminal domain responsible for oligomerization and RNP interaction.
Recombinant M1 protein is produced through genetic engineering, typically by cloning the M1 gene into expression vectors (e.g., bacterial, insect, or mammalian systems) to enable large-scale production. Escherichia coli-based systems are commonly used due to their cost-effectiveness and high yield, though post-translational modifications may require eukaryotic systems like baculovirus-insect cell cultures. Purification techniques, such as affinity chromatography, ensure high-purity M1 for research or therapeutic applications.
Studies on recombinant M1 have advanced understanding of influenza virus biology, including virion morphogenesis and host immune interactions. M1 is immunogenic, triggering cytotoxic T-cell responses, making it a candidate for universal influenza vaccine development. Additionally, recombinant M1 serves as a tool for diagnostic assays, antiviral drug screening, and structural studies (e.g., via X-ray crystallography or cryo-EM) to elucidate its conformational dynamics.
Recent research explores M1’s role in forming virus-like particles (VLPs) for vaccines and its potential as an adjuvant. Challenges remain in optimizing expression systems for native-like folding and post-translational modifications. Overall, recombinant M1 protein remains pivotal in virology, immunology, and therapeutic innovation against influenza.
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