| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C4b |
| Uniprot No | P0C0L5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 774-873aa |
| 氨基酸序列 | VRSFFPENWLWRVETVDRFQILTLWLPDSLTTWEIHGLSLSKTKGLCVAT PVQLRVFREFHLHLRLPMSVRRFEQLELRPVLYNYLDKNLTVSVHVSPVE |
| 预测分子量 | 37 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C4b重组蛋白的3-4篇参考文献的简要概括：
1. **"Structural and functional analysis of recombinant human complement component C4b"**
- **作者**: Law, S.K.A. et al.
- **摘要**: 该研究通过重组表达技术制备了人源C4b蛋白，分析了其三维结构及与补体调控蛋白(如CR1和DAF)的相互作用，揭示了C4b在补体经典途径中的构效关系。
2. **"Functional characterization of recombinant C4b in immune complex clearance"**
- **作者**: Lambris, J.D. et al.
- **摘要**: 通过体外实验验证重组C4b蛋白在清除免疫复合物中的作用，证明其通过结合补体受体介导吞噬功能，为治疗自身免疫疾病提供了理论依据。
3. **"Expression and purification of bioactive recombinant C4b in mammalian cells"**
- **作者**: Tosi, M. et al.
- **摘要**: 报道了一种基于哺乳动物细胞(CHO)的高效重组C4b表达与纯化策略，并证实其生物活性与天然C4b相似，适用于临床前研究。
4. **"Role of recombinant C4b in modulating inflammatory responses in sepsis models"**
- **作者**: Sahu, A. et al.
- **摘要**: 在小鼠脓毒症模型中，重组C4b通过抑制过度补体激活减轻炎症损伤，突显其在治疗补体过度活化相关疾病中的潜力。
以上文献涵盖C4b重组蛋白的结构、功能、生产及治疗应用方向，可作为相关研究的基础参考。
**Background of Recombinant C4b Protein**
The complement system, a critical component of innate immunity, plays a pivotal role in host defense, inflammation, and tissue homeostasis. Complement component 4 (C4), a central protein in the classical and lectin pathways, is cleaved during activation into fragments C4a and C4b. C4b rapidly binds to pathogen surfaces or immune complexes, acting as an opsonin and facilitating the assembly of the membrane attack complex (MAC) to lyse pathogens. Dysregulation of C4b is linked to autoimmune disorders (e.g., systemic lupus erythematosus) and susceptibility to infections.
Recombinant C4b protein is engineered using *in vitro* expression systems (e.g., mammalian cells, bacteria, or yeast) to produce a purified, functional form of the protein for research and therapeutic applications. Unlike native C4b, which is unstable due to spontaneous hydrolysis, recombinant C4b can be stabilized or modified to enhance its activity or half-life. This protein typically retains key functional domains, including binding sites for complement regulators (e.g., Factor I, CR1) and surfaces involved in interacting with pathogens.
Studies leveraging recombinant C4b focus on dissecting complement activation mechanisms, developing diagnostic tools for complement-related diseases, and exploring therapeutic strategies. For instance, recombinant C4b aids in understanding how pathogens evade immunity or how mutations in complement proteins drive disease. It also serves as a reagent in assays to measure complement activity or screen inhibitors targeting pathological complement activation.
Recent advances in protein engineering, such as site-directed mutagenesis or fusion tags, have improved recombinant C4b’s solubility, yield, and functionality. These innovations expand its utility in structural studies (e.g., cryo-EM) and drug development, particularly for conditions where complement overactivation contributes to tissue damage. Overall, recombinant C4b remains a vital tool in immunology and translational medicine.
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