| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | C39S |
| Uniprot No | Q99KQ4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-491aa |
| 氨基酸序列 | MNAAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFESREKKTENSKVRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKEVYREHFQDDVFNERGWNYILEKYDGHLPIEVKAVPEGSVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGIALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTEAPLIIRPDSGNPLDTVLKVLDILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKKWSIENVSFGSGGALLQKLTRDLLNCSFKCSYVVTNGLGVNVFKDPVADPNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGHDLLHTVFKNGKVTKSYSFDEVRKNAQLNIEQDVAPH |
| 预测分子量 | 60.6 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C39S重组蛋白的虚构参考文献示例(仅供格式参考，非真实文献)：
1. **文献名称**：*Structural and Functional Analysis of C39S Mutant Recombinant Protein in Bacterial Toxin Systems*
**作者**：Smith J. et al.
**摘要**：研究通过将细菌毒素复合物中的关键半胱氨酸(C39)突变为丝氨酸(S)，解析了C39S重组蛋白的结构稳定性及其对毒素分泌的影响，表明该突变降低了二硫键依赖性聚合。
2. **文献名称**：*C39S Recombinant Hydrolase Enhances Enzyme Activity under Oxidative Stress*
**作者**：Li Y. et al.
**摘要**：通过定点突变将水解酶的C39位点替换为丝氨酸，显著提高了该重组蛋白在氧化环境中的活性稳定性，为工业酶工程提供了优化策略。
3. **文献名称**：*Role of C39S Mutation in Recombinant Antimicrobial Peptide Production*
**作者**：Garcia R. et al.
**摘要**：探讨C39S重组抗菌肽的表达及纯化效率，发现该突变减少了宿主细胞内蛋白错误折叠，同时保留了抗菌活性。
4. **文献名称**：*C39S Recombinant Vaccine Antigen: Immunogenicity and Safety Evaluation*
**作者**：Wang H. et al.
**摘要**：开发基于C39S突变的病毒抗原重组蛋白，证明其在小鼠模型中诱导高效中和抗体且无毒性，具有疫苗开发潜力。
**注**：以上文献为示例，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“C39S recombinant protein”或结合具体研究领域筛选。
**Background of C39S Recombinant Protein**
The C39S recombinant protein is a genetically engineered variant of a native protein, typically derived from bacterial or eukaryotic expression systems, designed to study structure-function relationships or optimize stability and activity. The "C39S" nomenclature indicates a specific point mutation where the 39th amino acid residue, cysteine (C), is substituted with serine (S). This substitution often aims to eliminate reactive cysteine residues that may contribute to unwanted disulfide bond formation, oxidation-sensitive degradation, or interference with functional domains, thereby enhancing protein stability and solubility under experimental conditions.
Cysteine-to-serine mutations are common in protein engineering because serine shares structural similarity with cysteine (both contain hydroxyl/sulfhydryl groups) but lacks the thiol group’s redox reactivity. For example, in enzymes or binding proteins where cysteine residues are non-essential for catalytic activity or ligand interaction, the C39S mutation helps mitigate aggregation or inactivation during purification and storage. This variant is frequently utilized in biochemical assays, structural studies (e.g., crystallography), or therapeutic development, where consistent protein behavior is critical.
The recombinant protein is typically produced in *E. coli* or mammalian cell lines using plasmid vectors encoding the mutated sequence, followed by affinity chromatography purification (e.g., His-tag or GST-tag systems). Its applications span enzyme kinetics, inhibitor screening, antibody production, and molecular interaction analyses. By removing redox-sensitive cysteine residues, the C39S variant provides a more robust tool for research requiring long-term stability or reproducibility, particularly in oxidative environments. This mutation exemplifies rational protein design to balance functional integrity with practical experimental performance.
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