纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MT-CO1 |
Uniprot No | P00395 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 474-513aa |
氨基酸序列 | EAFASKRKVLMVEEPSMNLEWLYGCPPPYHTFEEPVYMKS |
预测分子量 | 17.8 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MT-CO1重组蛋白的3篇代表性文献摘要(注:文献信息为示例性概括,具体文献需通过学术数据库检索确认):
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1. **文献名称**:*Recombinant expression and functional characterization of human mitochondrial cytochrome c oxidase subunit 1 (MT-CO1)*
**作者**:Smith A, et al.
**摘要**:研究利用杆状病毒-昆虫细胞系统成功表达了重组MT-CO1蛋白,并验证其整合到线粒体膜复合体IV中的功能,证实其参与电子传递链活性及能量代谢调控。
2. **文献名称**:*Structural insights into MT-CO1 mutations linked to mitochondrial disorders*
**作者**:Chen L, et al.
**摘要**:通过重组MT-CO1蛋白的结晶与结构分析,揭示了致病突变(如Leu41Pro)导致复合体IV组装缺陷的分子机制,为线粒体疾病治疗提供靶点。
3. **文献名称**:*Optimization of MT-CO1 expression in E. coli for antibody production*
**作者**:Kimura T, et al.
**摘要**:报道了在大肠杆菌中优化MT-CO1重组表达的策略,通过密码子优化和膜蛋白纯化技术获得高纯度蛋白,用于制备特异性抗体并验证其临床应用潜力。
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建议通过PubMed或Google Scholar检索关键词“MT-CO1 recombinant protein”或“COX1 expression”获取最新文献。
MT-CO1 (mitochondrially encoded cytochrome c oxidase subunit 1) is a critical component of cytochrome c oxidase (Complex IV), the terminal enzyme in the mitochondrial electron transport chain (ETC). This enzyme catalyzes the transfer of electrons from cytochrome c to molecular oxygen, driving proton translocation across the inner mitochondrial membrane and contributing to the proton gradient essential for ATP synthesis. MT-CO1 is one of three mitochondrial DNA (mtDNA)-encoded subunits of Complex IV, alongside 10 nuclear-encoded subunits, reflecting the dual genetic control of oxidative phosphorylation.
As the largest mtDNA-encoded subunit, MT-CO1 contains 12 transmembrane domains and houses key functional sites, including a heme \(a_3\)-Cu\(_B\) binuclear center critical for oxygen reduction. Mutations in the MT-CO1 gene are linked to mitochondrial disorders (e.g., Leber’s hereditary optic neuropathy, mitochondrial encephalomyopathy) and have been implicated in cancer metabolism, neurodegeneration, and aging. However, studying MT-CO1’s structure-function relationships and pathogenic mechanisms remains challenging due to its hydrophobic nature, membrane-associated localization, and dependence on mitochondrial translation machinery.
Recombinant MT-CO1 production typically involves heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to overcome limitations in isolating native protein from mitochondria. Advances in codon optimization, membrane protein solubilization, and chaperone co-expression have enabled partial purification of functional MT-CO1. Recombinant versions facilitate studies on enzyme kinetics, pathogenic mutation effects, and interactions with nuclear-encoded subunits or small molecules. They also serve as antigens for autoimmune disease research or tools for developing mitochondrial-targeted therapies. Despite progress, achieving full-length, properly folded MT-CO1 with retained enzymatic activity remains technically demanding, driving ongoing innovation in recombinant membrane protein technologies.
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