| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CFD |
| Uniprot No | P00746 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-253aa |
| 氨基酸序列 | ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGK VQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKAT LGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLD RATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSG SRVCGNRKKPGIYTRVASYAAWIDSVLA |
| 预测分子量 | 26 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 **CFD(补体因子D)重组蛋白** 的参考文献示例(注：文献为虚构示例，仅作格式参考，建议通过学术数据库检索真实文献)：
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1. **标题**: *High-yield Expression and Purification of Recombinant Human Complement Factor D in Escherichia coli*
**作者**: Smith A, et al.
**摘要**: 研究报道了通过大肠杆菌系统高效表达重组人补体因子D的优化方法，采用亲和层析技术纯化，并验证其酶活性与天然蛋白一致，为大规模生产提供基础。
2. **标题**: *Structural Insights into Recombinant CFD in the Complement Alternative Pathway*
**作者**: Zhang L, et al.
**摘要**: 通过X射线晶体学解析重组CFD的三维结构，揭示了其与底物结合的活性位点特征，为开发补体系统相关疾病的靶向抑制剂提供结构基础。
3. **标题**: *Therapeutic Potential of Recombinant CFD Inhibitors in Age-related Macular Degeneration*
**作者**: Brown K, et al.
**摘要**: 利用重组CFD蛋白筛选小分子抑制剂，在动物模型中证明其可有效抑制补体替代通路过度激活，延缓视网膜病变进展。
4. **标题**: *Functional Characterization of Recombinant CFD in Autoimmune Disease Models*
**作者**: Tanaka M, et al.
**摘要**: 在类风湿关节炎小鼠模型中，重组CFD的基因递送显著降低补体介导的炎症反应，提示其作为免疫调节疗法的潜在价值。
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**建议**：通过PubMed、Web of Science或Google Scholar搜索关键词“recombinant complement factor D”或“CFD protein expression”，筛选近5年研究以获取最新进展。
**Background of Recombinant CFD Protein**
Complement Factor D (CFD), a serine protease in the complement system, plays a pivotal role in the alternative pathway of complement activation. It catalyzes the cleavage of Factor B, which, when bound to C3b, forms the C3 convertase (C3bBb), driving amplification of the complement cascade. This pathway is critical for immune defense but, when dysregulated, contributes to inflammatory and autoimmune diseases.
Recombinant CFD protein is engineered using biotechnological methods, such as expression in *E. coli* or mammalian cell systems, to produce highly pure, functional Factor D. Its production leverages gene cloning, vector design, and optimization of expression conditions to ensure proper folding and enzymatic activity. Unlike native Factor D, which circulates in low concentrations in plasma, recombinant CFD offers scalable and consistent yields, making it valuable for research and therapeutic applications.
Therapeutic interest in CFD stems from its role in complement-mediated pathologies. Inhibiting Factor D has emerged as a strategy to dampen excessive complement activation in conditions like paroxysmal nocturnal hemoglobinuria (PNH), age-related macular degeneration (AMD), and atypical hemolytic uremic syndrome (aHUS). Recombinant CFD is also used to study pathway mechanisms, screen inhibitors, and develop diagnostic assays.
Recent advancements include structural studies of CFD-inhibitor complexes to guide drug design and the development of long-acting biologics, such as monoclonal antibodies or small-molecule inhibitors. Additionally, recombinant CFD supports personalized medicine by enabling patient-specific studies of complement dysregulation.
Overall, recombinant CFD bridges basic research and clinical innovation, offering tools to unravel complement biology and therapies to target its pathogenic overactivity. Its applications highlight the intersection of immunology, biotechnology, and drug development in addressing complement-related diseases.
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