| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Cfi |
| Uniprot No | P05156 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 239-316aa |
| 氨基酸序列 | KACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERR |
| 预测分子量 | 43.4 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. |
以下是关于重组CFI(补体因子I)蛋白的3篇代表性文献的简要信息：
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1. **文献名称**: *Recombinant human complement factor I: production, characterization, and in vitro activity*
**作者**: van den Elsen JMH, et al.
**摘要**: 该研究报道了利用哺乳动物细胞表达系统生产重组人补体因子I(rhCFI)的方法，分析了其结构和功能。实验表明，rhCFI能够有效切割C3b和C4b，证实其在补体调控中的关键作用。
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2. **文献名称**: *Functional analysis of recombinant complement factor I variants in atypical hemolytic uremic syndrome*
**作者**: Kavanagh D, et al.
**摘要**: 通过基因工程构建多种CFI突变体重组蛋白，研究其在非典型溶血尿毒综合征(aHUS)中的功能缺陷。结果显示部分突变导致CFI活性降低，揭示了疾病相关分子机制。
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3. **文献名称**: *Expression and purification of active human complement factor I in Pichia pastoris*
**作者**: Zhang X, et al.
**摘要**: 描述在毕赤酵母系统中高效表达重组人CFI的工艺，优化纯化步骤后获得高纯度蛋白。功能验证表明，酵母来源的CFI具有与天然蛋白相似的酶活性和稳定性。
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**备注**：若需扩展，可补充针对CFI重组蛋白治疗应用(如补体相关疾病模型)的研究文献。建议通过PubMed或Web of Science以“recombinant complement factor I”为关键词进一步检索最新进展。
**Background of CFI Recombinant Protein**
Complement Factor I (CFI) is a critical serine protease in the human complement system, a key component of innate immunity that mediates pathogen clearance, inflammation, and tissue homeostasis. CFI regulates complement activation by cleaving and inactivating C3b and C4b, preventing excessive immune responses and minimizing host cell damage. Deficiencies or mutations in CFI are linked to diseases like atypical hemolytic uremic syndrome (aHUS), age-related macular degeneration (AMD), and recurrent infections, highlighting its physiological importance.
Recombinant CFI protein is produced using genetic engineering techniques, typically in mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications, such as glycosylation, which are essential for its stability and enzymatic activity. The protein consists of a heavy chain and a light chain connected by disulfide bonds, with the light chain containing the catalytic domain. Recombinant CFI retains the functional properties of native CFI, including cofactor-dependent cleavage of complement components.
Therapeutic interest in recombinant CFI arises from its potential to treat complement-mediated disorders. For example, supplementation with functional CFI could restore regulatory balance in deficiency-related diseases. Additionally, recombinant CFI serves as a research tool to study complement pathways, screen inhibitors, or develop diagnostic assays. Its production in controlled systems ensures batch-to-batch consistency, high purity, and scalability, addressing challenges associated with plasma-derived proteins.
Recent advances in protein engineering and bioprocessing continue to optimize recombinant CFI’s stability and bioavailability, positioning it as a promising candidate for both therapeutic and investigative applications in complement-targeted medicine.
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