| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C3 |
| Uniprot No | P01024 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 672-747aa |
| 氨基酸序列 | SVQLTEKRMDKVGKYPKELRKCCEDGMRENPMRFSCQRRTRFISLGEACK KVFLDCCNYITELRRQHARASHLGLA |
| 预测分子量 | 9 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C3重组蛋白的3篇示例参考文献(内容为虚构，仅供格式参考)：
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1. **文献名称**: *"Expression and Functional Characterization of Recombinant Human C3 Protein in HEK293 Cells"*
**作者**: Zhang, L., et al.
**摘要**: 本研究报道了在HEK293哺乳动物细胞中成功表达具有生物活性的重组人C3蛋白，并通过质谱和功能实验验证其与天然C3相似的补体激活能力，为补体系统研究提供工具。
2. **文献名称**: *"Structural Analysis of Recombinant C3 Reveals Key Domains for Complement Regulation"*
**作者**: Müller, R., & Tanaka, H.
**摘要**: 通过X射线晶体学解析重组C3蛋白的三维结构，揭示了其与补体调节因子(如Factor H)相互作用的关键结构域，为靶向补体通路的药物设计提供依据。
3. **文献名称**: *"Therapeutic Potential of Recombinant C3 Fusion Protein in Autoimmune Disease Models"*
**作者**: Chen, Y., et al.
**摘要**: 构建重组C3-免疫球蛋白融合蛋白，证明其在小鼠类风湿性关节炎模型中能选择性抑制补体过度激活，减少炎症损伤，提示其作为新型治疗分子的潜力。
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**注**：以上文献为示例性内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。
C3 recombinant protein is a engineered form of complement component 3 (C3), a central player in the complement system, which constitutes a critical arm of innate immunity. As the most abundant complement protein in human serum, native C3 (~185 kDa) is synthesized primarily in the liver and acts as a nexus for all complement activation pathways: classical, lectin, and alternative. Upon activation, C3 undergoes proteolytic cleavage into C3a (anaphylatoxin) and C3b (opsonin), mediating inflammatory responses, pathogen opsonization, and membrane attack complex formation.
The development of recombinant C3 emerged to address limitations in studying native C3's complex biology, particularly its rapid activation kinetics and short half-life. Using expression systems like mammalian cells (e.g., HEK293) or insect cells, researchers produce stable, modified C3 variants with controlled activation properties. Key technical challenges include preserving post-translational modifications (e.g., thioester bond formation critical for functionality) and achieving proper protein folding given its multi-domain structure (α- and β-chains connected by disulfide bonds).
Recombinant C3 has become indispensable for dissecting complement signaling mechanisms, developing therapeutic inhibitors for complement-mediated diseases (e.g., paroxysmal nocturnal hemoglobinuria, age-related macular degeneration), and engineering C3-derived proteins with tailored functions. Recent applications extend to biotechnology, where engineered C3 proteins are being explored as targeted immunomodulators in cancer therapy and as tools to improve biomaterial compatibility. Ongoing research focuses on creating hyperstable mutants and species-specific variants to facilitate translational studies, while CRISPR-edited cell lines are advancing large-scale production methods for clinical-grade material.
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