| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | clpC |
| Uniprot No | Q99W78 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-147aa |
| 氨基酸序列 | MLFGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLIGHGQDHVGTLHYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGNPEM |
| 预测分子量 | 32.4 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ClpC重组蛋白的3-4条参考文献及其简要摘要：
1. **文献名称**：*Structural insights into the ClpC ATPase activity and its regulation by the chaperone adaptor MecA*
**作者**：Kirstein, J., et al.
**摘要**：该研究通过X射线晶体学解析了枯草芽孢杆菌ClpC的ATP结合结构域结构，揭示了其ATP酶活性机制及MecA适配蛋白如何调控ClpC的底物识别与解折叠功能。
2. **文献名称**：*Reconstitution of a functional ClpC chaperone system in vitro*
**作者**：Schlothauer, T., et al.
**摘要**：报道了通过重组表达纯化ClpC及其共作用分子伴侣，在体外重建了具有底物解折叠活性的ClpC复合体，阐明了其依赖ATP的蛋白质质量控制机制。
3. **文献名称**：*Role of ClpC in stress response and virulence of Staphylococcus aureus*
**作者**：Frees, D., et al.
**摘要**：利用基因敲除和重组蛋白功能回补实验，证明ClpC在金黄色葡萄球菌耐热应激及致病性中的关键作用，揭示了其通过降解错误折叠蛋白维持细菌生存的分子途径。
4. **文献名称**：*Clp protease complexes and their role in bacterial proteostasis*
**作者**：Sauer, R.T., & Baker, T.A.
**摘要**：综述了ClpC与其他Clp蛋白酶(如ClpP)形成的复合体结构及其在细菌蛋白质稳态中的作用，强调重组ClpC在解析蛋白酶体功能及药物靶点开发中的应用。
(注：以上文献名称及作者为示例性内容，实际文献需根据具体数据库检索确认。)
ClpC recombinant protein is a key component of the ATP-dependent Clp protease system, primarily studied in bacteria such as *Bacillus subtilis* and *Streptomyces* species. As a member of the Hsp100/Clp family of AAA+ (ATPases Associated with diverse cellular Activities) proteins, ClpC functions as a regulatory ATPase that partners with the proteolytic subunit ClpP to form the ClpCP protease complex. This system plays a central role in protein quality control, stress response, and regulatory proteolysis by selectively degrading misfolded, damaged, or unnecessary proteins. ClpC recognizes substrate proteins tagged with specific degradation signals (e.g., ssrA tags) through its N-terminal domain, unfolds them via ATP hydrolysis, and translocates them into the ClpP chamber for proteolysis.
Recombinant ClpC is engineered for structural and functional studies using expression systems like *E. coli*, enabling large-scale purification for biochemical assays. Its hexameric structure, ATPase activity, and substrate interaction mechanisms are of significant interest in understanding bacterial stress adaptation and pathogenicity. In pathogens such as *Staphylococcus aureus* and *Mycobacterium tuberculosis*, ClpC is essential for survival under stress (e.g., heat, oxidative damage), making it a potential target for antimicrobial drug development. Inhibitors disrupting ClpC-ClpP interactions or ATPase activity could impair bacterial proteostasis, offering therapeutic strategies against antibiotic-resistant strains.
Research on recombinant ClpC also extends to biotechnology applications, including engineered protein degradation systems and synthetic biology tools. Its modular architecture and ATP-driven unfolding activity are exploited for controlled protein remodeling. However, challenges persist in elucidating substrate recognition specificity and regulatory mechanisms, necessitating further structural and kinetic analyses. Overall, ClpC recombinant protein serves as a critical model for studying bacterial proteolysis and advancing antimicrobial innovations.
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