| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SCO2 |
| Uniprot No | O43819 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 42-266aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGPAETGGQGQPQGPGLRTRLLITGLFGAG LGGAWLALRAEKERLQQQKRTEALRQAAVGQGDFHLLDHRGRARCKADFR GQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGLPPVQPVFITVDPE RDDVEAMARYVQDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPKDEDQDY IVDHSIAIYLLNPDGLFTDYYGRSRSAEQISDSVRRHMAAFRSVLS |
| 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SCO2重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅作格式参考)：
1. **文献名称**：*Expression and Functional Characterization of Recombinant Human SCO2 Protein in E. coli*
**作者**：Zhang L. et al.
**摘要**：本研究通过大肠杆菌表达系统成功制备了重组人SCO2蛋白，优化了纯化条件并验证其与铜离子结合的功能活性，为线粒体细胞色素c氧化酶(COX)组装机制研究提供工具。
2. **文献名称**：*Structural Insights into SCO2 Mutations Associated with Mitochondrial Disorders*
**作者**：Smith J.R., Brown K.T.
**摘要**：通过X射线晶体学解析了重组SCO2蛋白的三维结构，揭示了致病突变(如E140K)如何破坏蛋白构象，导致铜伴侣功能缺陷及COX组装异常。
3. **文献名称**：*Recombinant SCO2 Enhances Cellular Respiration and Reduces Oxidative Stress in Cardiomyocytes*
**作者**：Chen X. et al.
**摘要**：在心肌细胞中过表达重组SCO2蛋白，可显著提升线粒体呼吸链活性并降低ROS水平，提示其作为心力衰竭治疗的潜在靶点。
(注：若需真实文献，建议通过PubMed或Google Scholar搜索关键词“SCO2 recombinant protein”获取最新研究。)
**Background of SCO2 Recombinant Protein**
SCO2 (Synthesis of Cytochrome c Oxidase 2) is a mitochondrial protein critical for the biogenesis and function of cytochrome c oxidase (COX), the terminal enzyme in the mitochondrial electron transport chain (ETC). COX catalyzes the transfer of electrons to oxygen, a process essential for aerobic ATP production. SCO2 specifically facilitates the incorporation of copper ions into the COX catalytic core, a step vital for its enzymatic activity. Mutations in the *SCO2* gene are linked to severe mitochondrial disorders, such as infantile-onset COX deficiency, characterized by encephalomyopathy, cardiomyopathy, and early mortality.
Recombinant SCO2 protein is produced using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian cell lines), enabling large-scale purification for research. Its recombinant form retains the ability to bind copper and interact with COX assembly factors, making it a valuable tool for studying mitochondrial energy metabolism, metal ion homeostasis, and disease mechanisms. Researchers utilize SCO2 recombinant protein to investigate its structural dynamics, pathogenic mutations, and potential therapeutic strategies, including gene therapy or copper supplementation approaches. Additionally, it aids in screening compounds targeting COX dysfunction or mitochondrial disorders.
The study of SCO2 recombinant protein bridges gaps in understanding cellular bioenergetics and offers insights into developing treatments for mitochondrial diseases and age-related conditions linked to ETC impairments.
×
