纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CYC1 |
Uniprot No | P08574 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 85-325aa |
氨基酸序列 | SDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPEHDHRKRMGLKMLMMMALLVPLVYTIKRHKWSVLKSRKLAYRPPK |
预测分子量 | 54.4 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. |
以下为模拟生成的CYC1重组蛋白相关参考文献示例(非真实文献,供参考):
1. **《Functional expression and characterization of recombinant human cytochrome c1 (CYC1) in E. coli》**
- 作者:J. Smith et al.
- 摘要:研究利用大肠杆菌表达系统成功表达并纯化人源CYC1重组蛋白,通过光谱分析和酶活性测定验证其与天然蛋白功能的一致性,为线粒体复合体III的功能研究提供工具。
2. **《Structural insights into yeast CYC1 protein by recombinant expression and crystallography》**
- 作者:M. Tanaka & R. Wilson
- 摘要:通过酵母表达系统获得高纯度重组CYC1蛋白,结合X射线晶体学解析其三维结构,揭示其在线粒体电子传递链中的关键相互作用位点。
3. **《Site-directed mutagenesis of CYC1 reveals essential residues for electron transfer activity》**
- 作者:K. Lee et al.
- 摘要:通过定点突变技术构建CYC1突变体重组蛋白,发现His62和Met78残基对其与细胞色素c的结合及电子传递活性至关重要,为相关疾病的分子机制提供线索。
4. **《Recombinant CYC1 as a therapeutic target in mitochondrial dysfunction-related diseases》**
- 作者:A. Patel & S. Kumar
- 摘要:探讨重组CYC1蛋白在修复线粒体功能障碍中的作用,体外实验表明其可改善模型细胞的氧化磷酸化效率,提示潜在治疗神经退行性疾病的应用价值。
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建议通过PubMed、Web of Science等平台检索真实文献,关键词:**"CYC1 recombinant protein expression" / "Cytochrome c1 cloning"**。实际研究中,CYC1常与线粒体疾病、代谢工程或癌症研究相关。
CYC1 (Cytochrome c1), a key component of the mitochondrial electron transport chain (ETC), plays a critical role in cellular energy production. It is a subunit of Complex III (ubiquinol-cytochrome c reductase), facilitating electron transfer from ubiquinol to cytochrome c during oxidative phosphorylation. Encoded by the nuclear genome in eukaryotes, CYC1 is synthesized in the cytoplasm and imported into mitochondria, where it undergoes maturation, including heme group attachment and structural folding.
Recombinant CYC1 protein is engineered through heterologous expression systems (e.g., *E. coli* or yeast) to study its biochemical properties, interactions, and role in mitochondrial dysfunction. Its production enables detailed structural analysis (e.g., X-ray crystallography) and functional investigations into ETC disorders linked to mutations in CYC1 or associated assembly factors. Researchers also utilize recombinant CYC1 to develop disease models, particularly for mitochondrial encephalopathies and metabolic syndromes, and to screen therapeutic compounds targeting respiratory chain deficiencies.
Notably, recombinant CYC1 retains redox activity when properly folded, making it valuable for in vitro reconstitution of ETC complexes. Challenges in production include maintaining heme incorporation and ensuring correct disulfide bond formation, often addressed through co-expression with chaperones or optimized culture conditions. Its applications extend to antibody generation for diagnostic assays and CRISPR-based functional genomics studies. As mitochondrial research expands, recombinant CYC1 remains a pivotal tool for unraveling energy metabolism mechanisms and advancing precision medicine approaches for mitochondrial diseases.
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