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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CS |
| Uniprot No | Q9UFG5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-118aa |
| 氨基酸序列 | MGSKAKKRVL LPTRPAPPTV EQILEDVRGA PAEDPVFTIL APEDPPVPFR MMEDAEAPGE QLYQQSRAYV AANQRLQQAG NVLRQRCELL QRAGEDLERE VAQMKQAALP AAEAASSG |
| 预测分子量 | 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3篇与CS(Circumsporozoite)重组蛋白相关的模拟参考文献示例，涵盖不同研究方向：
1. **"Efficient expression and purification of Plasmodium falciparum CS recombinant protein in Escherichia coli"**
*作者：Zhang, L., Wang, Y., et al.*
摘要：研究通过优化大肠杆菌表达系统，实现了疟原虫环子孢子(CS)重组蛋白的高效可溶性表达，并开发了层析纯化策略，获得高纯度蛋白用于疫苗开发。
2. **"Structural and immunogenic characterization of a novel CS-based malaria vaccine candidate"**
*作者：Smith, J., Patel, R., et al.*
摘要：通过X射线晶体学解析了重组CS蛋白的抗原表位结构，结合小鼠模型验证其诱导强效中和抗体的能力，为新一代疟疾疫苗设计提供依据。
3. **"Yeast-derived recombinant CS protein production: Scale-up and process optimization"**
*作者：Kim, S., García-Sastre, A., et al.*
摘要：利用毕赤酵母系统实现CS重组蛋白的大规模生产，通过发酵条件优化使产量提升3倍，并证实其与哺乳动物细胞表达产物的免疫原性等效。
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*注：以上文献为示例，实际引用需查询具体数据库(如PubMed)。CS蛋白的缩写需根据研究领域明确(如本文假设为疟疾疫苗中的Circumsporozoite Protein)。*
**Background of CS Recombinant Proteins**
CS recombinant proteins, derived from the circumsporozoite (CS) antigen of *Plasmodium* parasites, have been a focal point in malaria vaccine development. The CS protein, expressed on the surface of sporozoites—the infective stage of malaria parasites transmitted by mosquitoes—plays a critical role in host cell invasion. Its central repeat region and conserved domains are essential for binding to hepatocytes, making it a prime target for neutralizing antibodies.
The concept of recombinant CS proteins emerged with advancements in genetic engineering, enabling large-scale production of pathogen-specific antigens in heterologous systems like *E. coli* or yeast. Recombinant technology offered a safer and more scalable alternative to traditional approaches using live or attenuated parasites. By cloning the CS gene into expression vectors, scientists could produce purified, stable proteins that retain immunogenic epitopes while eliminating infectious risks.
A landmark application is the RTS,S/AS01 vaccine, which fuses a portion of the CS protein (containing repeat and T-cell epitope regions) with the hepatitis B surface antigen. This chimeric protein, combined with adjuvant systems, induces antibody and cellular immune responses against the sporozoite stage. Clinical trials demonstrated partial efficacy, highlighting both the potential and limitations of CS-based vaccines.
Beyond malaria, CS recombinant proteins have inspired strategies against other infectious diseases, leveraging their ability to present conserved antigenic motifs. Challenges remain, including genetic variability of pathogens and suboptimal immune memory. Ongoing research focuses on optimizing protein design, adjuvant combinations, and multi-antigen platforms to enhance protection. Overall, CS recombinant proteins exemplify the intersection of molecular biology and immunology in combating global health threats.
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