| 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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艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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