| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | clpP2 |
| Uniprot No | O51698 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-198aa |
| 氨基酸序列 | MTGKEDNDACVLHDKSLKLVLKSRSIVIAGEITKDVSRLFQEKILLLEAL DFKKPIFVYIDSEGGDIDAGFAIFNMIRFVKPKVFTVGVGLVASAAALIF LAAKLENRFSLPFARYLLHQPLSGFKGVATDIEIYTNELNKVKKELNNII SKETGQKISKIEKDTDRDFWLDSSAAKKYGLVFEVVETKYQLEEFISA |
| 预测分子量 | 27 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ClpP2重组蛋白的3篇参考文献示例(注：以下内容为模拟生成，建议通过学术数据库验证真实性和准确性)：
1. **文献名称**: "Recombinant ClpP2 from Staphylococcus aureus: Expression and Enzymatic Characterization"
**作者**: Müller R, et al.
**摘要**: 研究在大肠杆菌中成功表达并纯化金黄色葡萄球菌ClpP2重组蛋白，证实其依赖ClpX的蛋白酶活性，并揭示其在细菌应激反应中的调控机制。
2. **文献名称**: "Cryo-EM Structure of the Arabidopsis ClpP2 Protease Complex"
**作者**: Zhang T, et al.
**摘要**: 通过冷冻电镜解析拟南芥ClpP2重组蛋白复合体的三维结构，阐明其与ClpT调控亚基的相互作用模式，为植物蛋白质稳态研究提供结构基础。
3. **文献名称**: "Targeting ClpP2 for Antimalarial Drug Discovery: Recombinant Protein Production and Inhibitor Screening"
**作者**: Kumar S, et al.
**摘要**: 开发疟原虫ClpP2重组蛋白的高效表达系统，筛选出小分子抑制剂，证明其通过破坏线粒体蛋白降解途径抑制寄生虫生长。
---
*注：实际文献需通过PubMed/Google Scholar检索关键词如"ClpP2 recombinant expression"或结合具体物种名称(如"Plasmodium ClpP2")获取。部分真实研究可能涉及ClpP与其他亚基共表达，建议结合实验目的筛选文献。*
**Background of ClpP2 Recombinant Protein**
ClpP2. a subunit of the Caseinolytic protease (Clp) system, is a highly conserved serine protease found in prokaryotes and eukaryotic organelles like mitochondria and chloroplasts. It forms a proteolytic core complex, typically associating with regulatory ATPase subunits (e.g., ClpX or ClpC) to create an ATP-dependent protease machinery. This system plays a critical role in protein quality control by degrading misfolded or damaged proteins, regulating stress responses, and maintaining cellular homeostasis. In bacteria, ClpP2 is often essential for virulence, making it a potential antimicrobial target.
Recombinant ClpP2 protein is produced via genetic engineering, often expressed in *E. coli* or other host systems, followed by purification using affinity chromatography. Structural studies reveal ClpP2 forms a tetradecameric ring structure with two heptameric rings stacked back-to-back, enclosing a proteolytic chamber. Its activity is tightly regulated, requiring partner ATPases for substrate recognition and unfolding. Dysregulation of ClpP2 has been linked to bacterial pathogenesis, mitochondrial disorders, and cancer, driving interest in its mechanistic study.
Research on recombinant ClpP2 focuses on elucidating its enzymatic mechanisms, substrate specificity, and interactions with regulatory partners. It also serves as a tool for drug discovery, particularly in developing antibiotics that disrupt bacterial ClpP complexes. Notably, ClpP2’s homolog in pathogens like *Staphylococcus aureus* and *Mycobacterium tuberculosis* is explored for novel therapies. In eukaryotes, mitochondrial ClpP2 mutations are associated with neurodegeneration and metabolic diseases, highlighting its biomedical relevance.
Overall, ClpP2 recombinant protein is pivotal for understanding proteostasis, microbial pathogenicity, and developing targeted therapeutics. Its conserved structure-function relationship across species underscores its evolutionary significance and versatility in cellular processes.
×
