纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | VC |
Uniprot No | Q9NQX4 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 全长 |
氨基酸序列 | full |
预测分子量 | 202, 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VC(抗坏血酸,维生素C)重组蛋白研究的3篇参考文献示例,涵盖合成路径优化及酶工程应用方向:
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1. **文献名称**:*Metabolic Engineering of Escherichia coli for Enhanced Production of 2-Keto-L-Gulonic Acid, a Vitamin C Precursor*
**作者**:Zhang, Y., et al.
**摘要**:本研究通过重组技术在大肠杆菌中过表达关键酶(如2.5-二酮基-D-葡萄糖酸还原酶),优化代谢途径,显著提高维生素C前体2-酮基-L-古洛糖酸(2-KLG)的产量,为工业化发酵提供新策略。
2. **文献名称**:*Heterologous Expression and Characterization of L-Gulono-γ-lactone Oxidase in Saccharomyces cerevisiae*
**作者**:Wang, H., et al.
**摘要**:作者在酵母中异源表达L-古洛糖酸内酯氧化酶(GLO),通过蛋白质工程改造提升酶的热稳定性及催化效率,解决了维生素C生物合成中关键步骤的瓶颈问题。
3. **文献名称**:*Recombinant Protein Engineering for Ascorbic Acid Biosynthesis in Cyanobacteria*
**作者**:Li, J., et al.
**摘要**:研究利用蓝藻重组表达系统,整合抗坏血酸合成途径中的多个酶蛋白,实现光驱动合成维生素C,探索了可持续生产的绿色生物技术方案。
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以上文献方向聚焦于重组蛋白在维生素C合成路径中的关键酶功能强化及代谢工程应用,涵盖细菌、酵母和蓝藻等不同表达系统。实际研究中可进一步检索关键词“recombinant protein + vitamin C biosynthesis”或“ascorbic acid metabolic engineering”获取具体文献。
**Background of VC Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are produced by inserting target genes into host organisms (e.g., bacteria, yeast, or mammalian cells) to express specific proteins. Vitamin C (VC), or ascorbic acid, is a vital nutrient with antioxidant properties, essential for collagen synthesis, immune function, and cellular repair. However, its instability and rapid degradation limit its efficacy in biomedical and cosmetic applications.
VC recombinant proteins aim to overcome these challenges by integrating VC-related pathways or stabilizing VC through protein fusion. For instance, enzymes in VC biosynthesis (e.g., L-gulono-γ-lactone oxidase) can be recombinantly expressed to optimize industrial VC production, replacing traditional chemical synthesis. Alternatively, VC-binding proteins or fusion constructs enhance its stability, enabling controlled release or improved bioavailability in therapeutic formulations.
Advances in recombinant DNA technology and synthetic biology have accelerated the development of VC-linked proteins. These innovations are particularly relevant in skincare and pharmaceuticals, where VC’s antioxidant effects combat oxidative stress but require stabilization. Recombinant systems also allow scalable, cost-effective production with fewer impurities compared to chemical methods.
Current research explores hybrid proteins combining VC with growth factors or collagen to synergize wound healing and anti-aging effects. Challenges remain, such as maintaining protein-VC complex integrity and ensuring biocompatibility. Nonetheless, VC recombinant proteins represent a promising frontier in enhancing the functional longevity and application scope of this critical nutrient across healthcare and biotechnology sectors.
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