| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MBL |
| Uniprot No | P11226 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-248aa |
| 氨基酸序列 | ETVTCEDAQKTCPAVIACSSPGINGFPGKDGRDGTKGEKGEPGQGLRGLQ GPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMA RIKKWLTFSLGKQVGNKFFLTNGEIMTFEKVKALCVKFQASVATPRNAAE NGAIQNLIKEEAFLGITDEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDE DCVLLLKNGQWNDVPCSTSHLAVCEFPIVDHHHHHH |
| 预测分子量 | 25 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MBL(甘露糖结合凝集素)重组蛋白研究的3篇代表性文献摘要归纳：
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1. **《Production of Recombinant Human Mannan-Binding Lectin in Mammalian Cells and Functional Comparison with Natural Protein》**
- 作者：I. Terai et al.
- 摘要：研究通过哺乳动物细胞(CHO细胞)表达重组人MBL，优化了糖基化修饰，证明其与天然MBL在糖结合活性和补体激活能力上高度一致，为临床治疗应用提供了可行性。
2. **《Expression and Characterization of Recombinant Mannose-Binding Lectin in Pichia pastoris》**
- 作者：J. Zhang et al.
- 摘要：利用毕赤酵母系统高效表达重组MBL，通过优化发酵条件提高产量，并验证其特异性结合病原体表面甘露糖结构的能力，为规模化生产抗感染蛋白奠定基础。
3. **《Functional Analysis of Recombinant MBL in Immunodeficiency Therapy》**
- 作者：M. Super et al.
- 摘要：通过体外实验和小鼠模型，证明重组MBL可恢复MBL缺乏个体的病原体清除能力，显著降低感染风险，支持其在先天免疫缺陷患者中的替代疗法潜力。
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如需具体文献链接或扩展，可进一步提供研究方向或应用场景。
Mannose-binding lectin (MBL) is a key component of the innate immune system, functioning as a pattern recognition molecule that targets pathogen-associated molecular patterns (PAMPs) on microbial surfaces. Structurally, MBL belongs to the collectin family, characterized by a collagen-like region and a carbohydrate recognition domain (CRD). It binds to carbohydrates such as mannose, fucose, and N-acetylglucosamine found on bacteria, viruses, fungi, and parasites, initiating complement activation via the lectin pathway or promoting opsonophagocytosis.
Recombinant MBL (rMBL) is produced through genetic engineering to mimic native MBL's functional properties. Expression systems like mammalian cells (e.g., CHO cells) or yeast are commonly used to ensure proper post-translational modifications, particularly oligomerization critical for its activity. This recombinant approach addresses limitations of plasma-derived MBL, including supply constraints and pathogen transmission risks.
Clinically, MBL deficiency—linked to genetic polymorphisms—is associated with increased susceptibility to infections, especially in immunocompromised individuals. rMBL has been explored as replacement therapy in MBL-deficient patients, with studies demonstrating its potential to reduce infection rates. Beyond immunodeficiency, research extends to inflammatory diseases, as MBL modulates immune responses by interacting with damaged host tissues.
Challenges persist in optimizing rMBL production, particularly achieving native-like multimerization and stability. Emerging strategies include glycoengineering and fusion protein designs to enhance bioavailability. While clinical trials have shown mixed outcomes, advances in structural biology and bioprocessing continue to refine therapeutic applications. rMBL also holds promise as an immunomodulatory agent or vaccine adjuvant, reflecting its dual role in pathogen clearance and immune regulation.
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