| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MR |
| Uniprot No | Q95460 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 201-300aa |
| 氨基酸序列 | TEPPLVRVNRKETFPGVTALFCKAHGFYPPEIYMTWMKNGEEIVQEIDYG DILPSGDGTYQAWASIELDPQSSNLYSCHVEHCGVHMVLQVPQESETIPL |
| 预测分子量 | 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. |
以下是关于甘露糖受体(Mannose Receptor, MR/CD206)重组蛋白研究的示例参考文献格式(内容为模拟构造，仅供参考)：
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1. **文献名称**：*Recombinant Human Mannose Receptor as a Targeted Drug Delivery System for Macrophages*
**作者**：Smith J. et al.
**摘要**：本研究成功表达并纯化了重组人甘露糖受体(rhMR)，验证其与甘露糖化抗原的特异性结合能力，并证明其在体外可定向递送药物至巨噬细胞，为炎症靶向治疗提供新策略。
2. **文献名称**：*Structural Characterization of the Mannose Receptor via X-ray Crystallography*
**作者**：Li Y. et al.
**摘要**：通过重组表达MR的胞外结构域，解析其晶体结构，揭示其糖类结合域的构象变化机制，为设计基于MR的免疫调节分子奠定结构基础。
3. **文献名称**：*Expression Optimization of Recombinant MR in Insect Cells for Functional Studies*
**作者**：Garcia R. et al.
**摘要**：利用杆状病毒-昆虫细胞系统优化MR重组蛋白表达条件，获得高活性蛋白，应用于病原体识别实验，证实其在先天免疫中的关键作用。
4. **文献名称**：*Role of Recombinant MR in Modulating Dendritic Cell Responses*
**作者**：Wang H. et al.
**摘要**：通过重组MR蛋白研究树突状细胞的抗原摄取机制，发现MR介导的内吞途径可增强抗原呈递效率，为疫苗佐剂开发提供依据。
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**注意**：以上文献为示例性内容，实际引用需通过学术数据库(如PubMed、Web of Science)检索关键词“Mannose Receptor recombinant protein”或“CD206 recombinant”获取真实文献。研究领域可涵盖结构生物学、药物递送、免疫调控等方向。
**Background of MR Recombinant Proteins**
Recombinant proteins, including MR (mannose receptor or other MR-designated proteins), are engineered through genetic modification to express specific functional molecules. The term "MR" may refer to various proteins, such as the mannose receptor (CD206), a key player in innate immunity, or other targets like the melanocortin receptor or multidrug resistance-associated proteins. These proteins are typically produced using recombinant DNA technology, where the gene encoding the target protein is cloned into a host organism (e.g., bacteria, yeast, or mammalian cells) to enable large-scale production.
The development of MR recombinant proteins stems from advances in molecular biology and biopharmaceutical research. For instance, the mannose receptor, a C-type lectin expressed on macrophages and dendritic cells, is crucial for pathogen recognition and antigen presentation. Recombinant versions of MR-related proteins have been instrumental in studying immune responses, vaccine development, and therapeutic interventions. Similarly, recombinant multidrug resistance-associated proteins are explored for their role in drug transport and cancer therapy resistance.
Applications of MR recombinant proteins span therapeutics, diagnostics, and research tools. They are used to design targeted therapies, such as receptor-blocking agents or drug delivery systems. In diagnostics, MR-based assays help detect biomarkers or pathogens. The production process involves optimizing expression systems to ensure proper folding, post-translational modifications, and functionality—challenges that vary depending on the protein’s complexity. Mammalian systems are often preferred for human-derived MR proteins requiring glycosylation.
Despite progress, challenges remain, including high production costs, scalability issues, and maintaining bioactivity. Ongoing innovations in synthetic biology, CRISPR editing, and AI-driven protein design aim to address these hurdles. MR recombinant proteins continue to hold promise in personalized medicine, infectious disease management, and oncology, reflecting their versatility in bridging basic science and clinical translation.
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