| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLPP |
| Uniprot No | Q16740 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-277aa |
| 氨基酸序列 | MWPGILVGGARVASCRYPALGPRLAAHFPAQRPPQRTLQNGLALQRCLHATATRALPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLVQKEPVEAAPAAEPVPAST |
| 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条关于CLPP重组蛋白的参考文献概览(信息基于真实研究领域，具体作者和期刊可能有调整)：
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1. **文献名称**：*Structural and functional insights into the recombinant human ClpP protease complex*
**作者**：Kirstein J. et al.
**摘要**：研究通过重组表达人源CLPP蛋白，解析其晶体结构，揭示其底物识别和ATP依赖性水解机制，为调控线粒体蛋白质量控制提供结构基础。
2. **文献名称**：*Mitochondrial CLPP modulates ROS production and apoptosis via selective degradation of unfolded proteins*
**作者**：Szczepanowska K. et al.
**摘要**：利用重组CLPP蛋白验证其在线粒体应激中的功能，证明其通过降解错误折叠蛋白调控活性氧(ROS)平衡，影响细胞凋亡通路。
3. **文献名称**：*Recombinant CLPP restores mitochondrial function in a cellular model of Perrault syndrome*
**作者**：Bakshi R. et al.
**摘要**：通过体外重组CLPP蛋白递送至CLPP缺陷细胞，恢复线粒体蛋白水解活性，为遗传性疾病(如Perrault综合征)的基因治疗提供实验依据。
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**注**：以上文献名称和作者为示例性质，建议通过PubMed或Google Scholar以关键词“CLPP recombinant protein”或“CLPP protease function”检索最新具体文献。
CLPP (Caseinolytic Mitochondrial Matrix Peptidase Proteolytic Subunit) is a highly conserved ATP-dependent protease belonging to the Clp protease family, primarily localized in the mitochondrial matrix. It plays a critical role in maintaining mitochondrial proteostasis by degrading misfolded, damaged, or surplus proteins. Structurally, CLPP forms a ring-shaped tetradecameric complex, often working in concert with regulatory ATPase subunits like CLPX or CLPA to recognize and process substrates. Its proteolytic activity is essential for mitochondrial protein quality control, stress response, and metabolic regulation, particularly under conditions such as oxidative stress or energy deprivation.
Recombinant CLPP proteins are engineered using heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to study its biochemical functions, substrate specificity, and interactions. These proteins enable researchers to dissect CLPP's role in mitochondrial dynamics, apoptosis, and diseases linked to mitochondrial dysfunction, including neurodegenerative disorders (e.g., Parkinson’s disease), cancer, and metabolic syndromes. For instance, CLPP dysregulation has been implicated in impaired clearance of toxic protein aggregates, contributing to disease progression.
The production of recombinant CLPP involves codon optimization, affinity tag fusion (e.g., His-tag), and chromatographic purification, often followed by activity assays to validate functionality. Its applications span structural studies (cryo-EM, X-ray crystallography), drug screening for CLPP modulators, and gene therapy research. Challenges remain in maintaining the protein’s native conformation and activity *in vitro*, as well as understanding tissue-specific regulatory mechanisms. Ongoing research aims to leverage recombinant CLPP for therapeutic strategies targeting mitochondrial disorders and aging-related pathologies.
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