| 纯度 | >85%SDS-PAGE. |
| 种属 | rat |
| 靶点 | MBL1 |
| Uniprot No | P19999 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-238 |
| 氨基酸序列 | SGS QTCEETLKTC SVIACGRDGR DGPKGEKGEP GQGLRGLQGP PGKLGPPGSV GAPGSQGPKG QKGDRGDSRA IEVKLANMEA EINTLKSKLE LTNKLHAFSM GKKSGKKFFV TNHERMPFSK VKALCSELRG TVAIPRNAEE NKAIQEVAKT SAFLGITDEV TEGQFMYVTG GRLTYSNWKK DEPNDHGSGE DCVTIVDNGL WNDISCQASH TAVCEFPA |
| 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MBL1重组蛋白的示例参考文献(注：以下为模拟文献，实际文献需通过学术数据库检索获取)：
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1. **标题**: *"Expression and functional characterization of recombinant porcine MBL1 in Escherichia coli"*
**作者**: Zhang Y, et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了重组猪MBL1蛋白，验证了其碳水化合物结合活性及补体激活能力，证明其在先天免疫中的潜在应用价值。
2. **标题**: *"Structural analysis of MBL1 reveals key residues for pathogen recognition in swine"*
**作者**: Smith JL, et al.
**摘要**: 通过X射线晶体学解析猪MBL1的碳水化合物识别结构域(CRD)，揭示了其与病原体表面甘露糖特异性结合的分子机制，为抗病育种提供理论依据。
3. **标题**: *"Recombinant MBL1 enhances opsonization of Streptococcus suis in vitro"*
**作者**: Tanaka K, et al.
**摘要**: 体外实验表明，重组MBL1能显著增强猪肺泡巨噬细胞对猪链球菌的吞噬作用，提示其在细菌感染中的免疫调节功能。
4. **标题**: *"Development of a mammalian cell system for high-yield production of glycosylated MBL1"*
**作者**: Müller R, et al.
**摘要**: 报道了一种基于HEK293细胞的哺乳动物表达系统，用于生产糖基化修饰的重组MBL1.优化后的蛋白表现出更接近天然构象的稳定性和生物活性。
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**建议**：可通过PubMed、Google Scholar等平台搜索关键词“recombinant MBL1”、“porcine MBL1”或“MBL1 protein expression”获取真实文献。
**Background of MBL1 Recombinant Protein**
Mannose-binding lectin 1 (MBL1), a member of the collectin family, is a key pattern recognition molecule in the innate immune system. It plays a critical role in pathogen recognition by binding to carbohydrate structures (e.g., mannose, fucose, N-acetylglucosamine) on microbial surfaces, such as bacteria, viruses, fungi, and parasites. This binding triggers complement activation via the lectin pathway, enhancing opsonization and clearance of pathogens. Structurally, MBL1 forms oligomers composed of identical subunits, each containing a collagen-like region and a carbohydrate-recognition domain (CRD). Genetic polymorphisms in the *MBL1* gene can influence protein levels and functional efficiency, impacting susceptibility to infections.
Recombinant MBL1 protein is produced using biotechnological platforms (e.g., mammalian or insect cell systems) to mimic the native protein’s structure and activity. It retains the ability to form oligomers and bind pathogens, making it a valuable tool for studying immune responses, host-pathogen interactions, and complement activation mechanisms. Its applications extend to therapeutic development, particularly in addressing MBL deficiency-associated immunocompromised conditions or as an adjuvant in antimicrobial therapies.
Research on recombinant MBL1 also explores its role in modulating inflammation and autoimmune diseases, given its dual capacity to enhance microbial clearance and regulate immune overactivation. Challenges remain in optimizing production yield, stability, and post-translational modifications (e.g., glycosylation) to ensure functional consistency. Overall, recombinant MBL1 bridges translational gaps in immunology and offers potential for novel therapeutic strategies against infectious and inflammatory disorders.
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