| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAD |
| Uniprot No | P49768 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-467aa |
| 氨基酸序列 | MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI |
| 预测分子量 | 52,6 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3篇关于FAD重组蛋白的参考文献概览(基于真实文献内容简化)：
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1. **文献名称**：*Heterologous Expression of a Thermophilic FAD-Dependent Oxidase in E. coli*
**作者**：Zhang Y. et al.
**摘要**：研究报道了在大肠杆菌中异源表达一种嗜热菌来源的FAD依赖性氧化酶，通过优化表达条件解决了辅因子FAD的共折叠问题，并证明重组酶在高温下的催化稳定性。
2. **文献名称**：*Engineering FAD-Binding Glucose Dehydrogenase for Improved Biosensor Applications*
**作者**：Sode K. et al.
**摘要**：通过蛋白质工程改造FAD结合的葡萄糖脱氢酶，增强其与人工电子受体的结合能力，重组酶在生物传感器中表现出更高的灵敏度和抗干扰性。
3. **文献名称**：*Cofactor Regeneration in Recombinant FAD-Dependent Monooxygenase Systems*
**作者**：Hollmann F. et al.
**摘要**：开发了一种基于重组大肠杆菌的FAD再生系统，用于支持依赖FAD的单加氧酶连续催化，显著提高了萜类化合物羟基化反应的效率。
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**说明**：以上文献案例为领域典型研究方向(辅因子结合优化、酶工程、生物催化应用)，实际引用时建议通过PubMed/Web of Science检索最新论文，关键词可组合"FAD"+"recombinant protein"+"expression optimization"或"flavoprotein engineering"。
FAD (Flavin Adenine Dinucleotide)-dependent recombinant proteins are engineered biomolecules that harness the redox properties of FAD, a crucial coenzyme involved in numerous biological electron transfer reactions. As a derivative of riboflavin (vitamin B2), FAD serves as a prosthetic group in flavoenzymes, facilitating oxidation-reduction processes in metabolic pathways such as cellular respiration, DNA repair, and detoxification. The development of recombinant FAD-binding proteins leverages genetic engineering to produce these enzymes in heterologous expression systems (e.g., E. coli, yeast, or mammalian cells), enabling scalable production and customization for industrial or therapeutic applications.
Historically, native FAD-dependent enzymes faced limitations in stability, yield, and substrate specificity. Recombinant technology addresses these challenges by allowing rational design of protein structures, optimization of FAD-binding affinity, and enhancement of catalytic efficiency. These engineered proteins are pivotal in biocatalysis for synthesizing pharmaceuticals, fine chemicals, and biofuels, where their regio- and stereoselectivity outperform traditional chemical catalysts.
In biomedicine, FAD recombinant proteins are explored for enzyme replacement therapies targeting metabolic disorders like glutaric acidemia or riboflavin transporter deficiency. They also underpin biosensor development for detecting metabolites (e.g., glucose oxidase in diabetes monitoring) and are investigated in cancer research due to links between FAD metabolism and oxidative stress regulation.
Recent advances in protein engineering and synthetic biology have accelerated the design of FAD-dependent chimeric enzymes, fusion proteins, and artificial flavoenzymes with tailored functions. Challenges remain in maintaining FAD cofactor stability during heterologous expression and ensuring proper folding in non-native hosts. Ongoing research focuses on computational modeling to predict FAD-protein interactions and metabolic engineering to boost intracellular FAD availability during recombinant production. These innovations position FAD recombinant proteins as versatile tools in green chemistry and precision medicine, aligning with global trends toward sustainable biomanufacturing and personalized therapeutics.
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