| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FCN2 |
| Uniprot No | Q15485 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-313aa |
| 氨基酸序列 | LQAADTCPEVKMVGLEGSDKLTILRGCPGLPGAPGPKGEAGTNGKRGERGPPGPPGKAGPPGPNGAPGEPQPCLTGPRTCKDLLDRGHFLSGWHTIYLPDCRPLTVLCDMDTDGGGWTVFQRRVDGSVDFYRDWATYKQGFGSRLGEFWLGNDNIHALTAQGTSELRVDLVDFEDNYQFAKYRSFKVADEAEKYNLVLGAFVEGSAGDSLTFHNNQSFSTKDQDNDLNTGNCAVMFQGAWWYKNCHVSNLNGRYLRGTHGSFANGINWKSGKGYNYSYKVSEMKVRPA |
| 预测分子量 | 33.4kDa |
| 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FCN2重组蛋白的3篇参考文献，按文献名称、作者及摘要内容概括整理：
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1. **文献名称**：*Production and functional characterization of recombinant human Ficolin-2*
**作者**：Matsushita M, et al.
**摘要**：研究报道了在哺乳动物细胞(CHO细胞)中成功表达重组人FCN2蛋白，证实其能结合病原体表面糖结构(如乙酰化分子)，并通过凝集素途径激活补体系统，为研究FCN2的免疫功能提供工具。
2. **文献名称**：*Recombinant Ficolin-2 enhances phagocytosis and killing of Streptococcus pneumoniae by macrophages*
**作者**：Kjaer TR, et al.
**摘要**：通过大肠杆菌系统表达FCN2重组蛋白，发现其可增强巨噬细胞对肺炎链球菌的吞噬及杀伤能力，揭示了FCN2在抗细菌感染中的调理素作用机制。
3. **文献名称**：*Structural insights into Ficolin-2 oligomerization and pathogen recognition*
**作者**：Garlatti V, et al.
**摘要**：利用昆虫细胞表达系统获得重组FCN2蛋白，通过X射线晶体学解析其三维结构，阐明其多聚化模式及与病原体配体结合的关键结构域，为设计靶向免疫疗法提供依据。
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以上文献涵盖FCN2重组蛋白的表达系统开发(CHO、大肠杆菌、昆虫细胞)、免疫功能验证(补体激活、病原清除)及结构解析，适用于基础研究与药物开发参考。
FCN2 (ficolin-2), a member of the fibrinogen-related protein family, is a soluble pattern recognition molecule central to innate immunity. Produced primarily in the liver and secreted into the bloodstream, it acts as a key component of the lectin complement pathway. FCN2 binds to pathogen-associated molecular patterns (PAMPs) on microbial surfaces, such as acetylated sugars (e.g., GlcNAc) or lipoteichoic acid, through its fibrinogen-like domain. This binding triggers complement activation via associated serine proteases (MASPs), leading to pathogen opsonization, inflammation, and targeted cell lysis.
Recombinant FCN2 proteins are engineered to study its structural and functional properties. They are typically expressed in mammalian cell systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, including glycosylation, which is critical for ligand binding and stability. Alternatively, bacterial systems may be used for truncated forms focused on specific domains. These recombinant variants enable detailed investigations into FCN2’s interactions with pathogens, host cells, and complement components.
Research highlights FCN2’s dual role in immunity: protective against bacterial/viral infections (e.g., *Streptococcus*, influenza) and implicated in autoimmune diseases (e.g., rheumatoid arthritis) due to aberrant complement activation. Polymorphisms in the *FCN2* gene correlate with disease susceptibility, driving interest in recombinant FCN2 for diagnostic or therapeutic applications. Recent studies explore its potential as a biomarker for sepsis or as a modulator of immune responses in transplantation. Challenges remain in optimizing recombinant production to mirror native protein functionality, particularly in multimer formation essential for pathogen recognition. Advances in protein engineering may unlock therapeutic strategies harnessing FCN2’s pathogen-targeting capabilities.
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