| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MLEC |
| Uniprot No | Q14165 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-269aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSPGLGVAG VAGAAGAGLP ESVIWAVNAG GEAHVDVHGI HFRKDPLEGR VGRASDYGMK LPILRSNPED QILYQTERYN EETFGYEVPI KEEGDYVLVL KFAEVYFAQS QQKVFDVRLN GHVVVKDLDI FDRVGHSTAH DEIIPMSIRK GKLSVQGEVS TFTGKLYIEF VKGYYDNPKV CALYIMAGTV DDVPKLQPHP GLEKKEEEEE EEEYDEGSNL KKQTNKNRVQ SGPRTPNPYA SDNS |
| 预测分子量 | 29 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MLEC重组蛋白的3篇示例参考文献(注：以下为虚构文献，仅作格式示例参考)：
1. **文献名称**: *Expression and Functional Characterization of MLEC Recombinant Protein in Mammalian Cells*
**作者**: Zhang, Y. et al.
**摘要**: 研究通过哺乳动物表达系统成功表达MLEC重组蛋白，验证其与特定受体的结合活性，并证明其在体外模型中抑制炎症反应的潜力。
2. **文献名称**: *Structural Insights into MLEC Protein via Cryo-EM Analysis*
**作者**: Tanaka, K. et al.
**摘要**: 利用冷冻电镜技术解析MLEC重组蛋白的高分辨率结构，揭示其功能域的空间构象，为靶向药物设计提供结构基础。
3. **文献名称**: *MLEC-Fc Fusion Protein Enhances Immune Response in Vaccine Development*
**作者**: Patel, R. et al.
**摘要**: 构建MLEC与Fc片段的重组融合蛋白，在小鼠模型中证明其作为疫苗佐剂可显著提升抗原特异性抗体水平。
4. **文献名称**: *Optimization of MLEC Recombinant Production in E. coli for Industrial Applications*
**作者**: Schmidt, H. et al.
**摘要**: 通过优化大肠杆菌表达条件和纯化工艺，大幅提高MLEC蛋白的产量和稳定性，为其规模化生产提供可行方案。
(如需真实文献，建议通过PubMed或Google Scholar检索关键词“MLEC recombinant protein”获取最新研究。)
**Background of MLEC Recombinant Protein**
MLEC (Mannose-binding lectin, also known as mannan-binding lectin) is a key component of the innate immune system, primarily involved in pathogen recognition and activation of the complement system. Structurally, MLEC belongs to the collectin family, characterized by collagen-like domains and carbohydrate-recognition domains (CRDs) that bind to specific sugar patterns on microbial surfaces, such as mannose, fucose, and N-acetylglucosamine. This binding triggers opsonization and activates the lectin complement pathway, enhancing immune responses against pathogens.
Recombinant MLEC (rMLEC) is produced using genetic engineering techniques, often expressed in mammalian cell systems (e.g., CHO or HEK293 cells) or bacterial systems (e.g., E. coli) to ensure proper folding and post-translational modifications. The recombinant form retains the functional properties of native MLEC, including oligomerization and carbohydrate-binding activity, while offering advantages like high purity, scalability, and reduced batch variability.
Research on rMLEC has expanded its applications beyond basic immunology. It is studied for therapeutic potential in conditions linked to MBL deficiency, which increases susceptibility to infections and autoimmune diseases. Additionally, rMLEC serves as a tool to investigate host-pathogen interactions, vaccine development, and as a diagnostic marker for immune disorders. Engineering efforts focus on modifying its stability or binding specificity to enhance clinical utility, such as in targeted drug delivery or as an adjuvant in immunotherapy. Overall, rMLEC exemplifies the intersection of structural biology, immunology, and biotechnology in advancing therapeutic and diagnostic innovations.
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