| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ubiC |
| Uniprot No | P26602 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-165aa |
| 氨基酸序列 | SHPALTQLRALRYCKEIPALDPQLLDWLLLEDSMTKRFEQQGKTVSVTMIREGFVEQNEIPEELPLLPKESRYWLREILLCADGEPWLAGRTVVPVSTLSGPELALQKLGKTPLGRYLFTSSTLTRDFIEIGRDAGLWGRRSRLRLSGKPLLLTELFLPASPLY |
| 预测分子量 | 19.5 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 **ubiC重组蛋白** 的模拟参考文献示例(仅供参考，实际文献请通过学术数据库查询)：
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1. **文献名称**：*Cloning and Heterologous Expression of the ubiC Gene from Escherichia coli for 4-Hydroxybenzoic Acid Biosynthesis*
**作者**：R. Meganathan, et al.
**摘要**：研究报道了大肠杆菌ubiC基因的克隆及其在异源宿主中的重组表达，验证了该基因编码的4-羟基苯甲酸酯八烯基转移酶在辅酶Q生物合成中的功能。
2. **文献名称**：*Enzymatic Characterization of Recombinant UbiC: A Key Enzyme in Ubiquinone Pathway*
**作者**：Y. Zhang, et al.
**摘要**：通过重组表达纯化UbiC蛋白，分析了其酶动力学特性及对底物4-羟基苯甲酸的催化效率，揭示了其在辅酶Q合成中的关键作用。
3. **文献名称**：*Structural Insights into UbiC Protein via X-ray Crystallography: Implications for Substrate Binding*
**作者**：S. Lee, et al.
**摘要**：解析了重组UbiC蛋白的晶体结构，阐明了其活性位点与底物结合机制，为酶工程改造提供了结构基础。
4. **文献名称**：*Enhanced Coenzyme Q10 Production by Overexpression of Recombinant UbiC in Engineered Escherichia coli*
**作者**：H. Wang, et al.
**摘要**：通过代谢工程策略过表达重组UbiC蛋白，显著提高了大肠杆菌中辅酶Q10的产量，展示了其在工业生物技术中的应用潜力。
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**注意**：以上文献为模拟示例，实际研究需查阅真实数据库(如PubMed、Web of Science)。建议结合关键词“ubiC recombinant protein”“4-hydroxybenzoate octaprenyltransferase”进行检索。
The ubiC gene, derived from *Escherichia coli*, encodes chorismate lyase (UbiC), a critical enzyme in the ubiquinone (coenzyme Q) biosynthesis pathway. UbiC catalyzes the cleavage of chorismate, a central intermediate in aromatic amino acid metabolism, into 4-hydroxybenzoate and pyruvate. This reaction represents the first committed step in the production of ubiquinone, an essential lipid-soluble electron carrier in aerobic respiration and oxidative phosphorylation. Due to its role in energy metabolism and cellular redox balance, UbiC has attracted interest in both basic research and biotechnological applications.
Recombinant UbiC protein is typically produced via heterologous expression in bacterial systems such as *E. coli*. Cloning the ubiC gene into expression vectors under inducible promoters (e.g., T7 or lac) enables high-yield protein production. Purification methods often employ affinity tags (e.g., His-tag) followed by chromatography, yielding soluble and active enzyme preparations. Structural studies using X-ray crystallography have revealed UbiC's homodimeric architecture and catalytic mechanism, providing insights into substrate specificity and potential engineering strategies.
Research on recombinant UbiC focuses on its enzymatic properties, regulatory mechanisms, and applications in synthetic biology. It serves as a model enzyme for studying chorismate-utilizing pathways and has been explored in metabolic engineering to enhance ubiquinone production for industrial or therapeutic purposes. Additionally, UbiC's role in microbial metabolism positions it as a potential target for antimicrobial agents, particularly against pathogens relying on endogenous ubiquinone synthesis. Its stability and catalytic efficiency also make it a candidate for biocatalytic processes in fine chemical synthesis. Overall, recombinant UbiC represents a versatile tool bridging microbial physiology studies and biotechnological innovation.
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