| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SCO1 |
| Uniprot No | O75880 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 132-301aa |
| 氨基酸序列 | MGKPLLGGPF SLTTHTGERK TDKDYLGQWL LIYFGFTHCP DVCPEELEKM IQVVDEIDSI TTLPDLTPLF ISIDPERDTK EAIANYVKEF SPKLVGLTGT REEVDQVARA YRVYYSPGPK DEDEDYIVDH TIIMYLIGPD GEFLDYFGQN KRKGEIAASI ATHMRPYRKK SLEHHHHHH |
| 预测分子量 | 21 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SCO1重组蛋白的3篇参考文献示例(注：文献为虚构示例，实际引用时请核实真实来源)：
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1. **标题**: *Structural and Functional Analysis of Human SCO1 Recombinant Protein in Mitochondrial Copper Homeostasis*
**作者**: Chen, L., et al.
**摘要**: 本研究通过大肠杆菌表达并纯化了重组人SCO1蛋白，结合X射线晶体学揭示了其铜结合结构域的关键位点，证实SCO1在细胞色素c氧化酶(COX)组装中通过铜离子转运调控线粒体呼吸链功能。
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2. **标题**: *Recombinant SCO1 Rescues Copper Deficiency in a Zebrafish Model of SCO1 Deficiency*
**作者**: Rodriguez, J.A., et al.
**摘要**: 利用重组SCO1蛋白在斑马鱼模型中验证其功能，证明外源性SCO1能恢复因基因突变导致的COX活性缺陷，为相关线粒体疾病的治疗提供实验依据。
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3. **标题**: *In Vitro Reconstitution of SCO1- SCO2 Interaction Using Purified Recombinant Proteins*
**作者**: Müller, P., et al.
**摘要**: 通过共表达纯化SCO1和SCO2重组蛋白，发现两者在铜离子存在下形成复合物，并协同参与COX亚基的金属化过程，揭示了二者在氧化酶组装中的协同机制。
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**注意**：以上文献信息为示例，实际研究中请通过PubMed、Web of Science等数据库检索真实文献。关键词建议：**SCO1 recombinant protein expression**、**SCO1 copper binding**、**cytochrome c oxidase assembly**。
**Background of SCO1 Recombinant Protein**
SCO1 (Synthesis of Cytochrome c Oxidase 1) is a mitochondrial protein essential for the assembly and function of cytochrome c oxidase (COX), the terminal enzyme in the electron transport chain responsible for aerobic ATP production. As a copper chaperone, SCO1 facilitates the delivery of copper ions to the catalytic subunits of COX, particularly COX II, ensuring proper metallation and enzymatic activity. This process is critical for oxidative phosphorylation and cellular energy homeostasis.
Mutations in the *SCO1* gene are linked to severe human disorders, such as early-onset mitochondrial encephalopathy, hepatic failure, and hypertrophic cardiomyopathy, underscoring its physiological importance. To study SCO1’s molecular mechanisms and disease-related pathologies, recombinant SCO1 proteins are generated using heterologous expression systems (e.g., *E. coli* or mammalian cell cultures). These recombinant variants retain the conserved twin CX3C motif involved in copper binding and protein-protein interactions.
Research on SCO1 recombinant proteins has illuminated its dual role in copper trafficking and redox regulation. Structural analyses reveal dynamic conformational changes during copper transfer, while biochemical studies highlight interactions with COX assembly factors like COX17 and SCO2. Additionally, recombinant SCO1 serves as a tool to investigate mitochondrial copper metabolism dysregulation in neurodegenerative diseases and cancer.
Challenges in producing functional recombinant SCO1 include preserving its redox-sensitive disulfide bonds and copper-binding capacity, often requiring optimized expression conditions and chaperone co-expression. Despite these hurdles, SCO1 recombinant proteins remain pivotal in advancing therapeutic strategies targeting mitochondrial disorders.
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