| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FMO1 |
| Uniprot No | Q01740 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-532aa |
| 氨基酸序列 | MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYSDFPFPEDYPNYVPNSQFLEYLKMYANHFDLLKHIQFKTKVCSVTKCSDSAVSGQWEVVTMHEEKQESAIFDAVMVCTGFLTNPYLPLDSFPGINAFKGQYFHSRQYKHPDIFKDKRVLVIGMGNSGTDIAVEASHLAEKVFLSTTGGGWVISRIFDSGYPWDMVFMTRFQNMLRNSLPTPIVTWLMERKINNWLNHANYGLIPEDRTQLKEFVLNDELPGRIITGKVFIRPSIKEVKENSVIFNNTSKEEPIDIIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAIIGLIKPLGSMIPTGETQARWAVRVLKGVNKLPPPSVMIEEINARKENKPSWFGLCYCKALQSDYITYIDELLTYINAKPNLFSMLLTDPHLALTVFFGPCSPYQFRLTGPGKWEGARNAIMTQWDRTFKVIKARVVQESPSPFESFLKVFSFLALLVAIFLIFL |
| 预测分子量 | 60,3 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FMO1重组蛋白的3篇代表性文献及其摘要概述：
1. **"Functional expression of human flavin-containing monooxygenase 1 (FMO1) in Escherichia coli"**
- **作者**: Zhang, J., Cashman, J.R.
- **摘要**: 研究报道了通过大肠杆菌系统成功表达重组人源FMO1蛋白，并验证其催化氧化硫/氮化合物的活性，为后续酶学机制研究提供工具。
2. **"Purification and characterization of recombinant rabbit FMO1: substrate specificity and thermal stability analysis"**
- **作者**: Krueger, S.K., Williams, D.E.
- **摘要**: 利用杆状病毒-昆虫细胞系统表达兔源FMO1.纯化后分析其底物选择性和热稳定性，揭示了物种间酶活差异及潜在药物代谢应用价值。
3. **"Structural insights into FMO1 catalysis through recombinant protein crystallization"**
- **作者**: Alfieri, A., et al.
- **摘要**: 通过重组FMO1蛋白的结晶和X射线衍射分析，解析其三维结构，阐明辅因子FAD结合域及底物通道的关键氨基酸位点。
注：以上文献信息为示例性质，实际引用需核实具体文献来源及内容准确性。
**Background of FMO1 Recombinant Protein**
Flavin-containing monooxygenase 1 (FMO1) is a member of the FMO enzyme family, which plays a critical role in the oxidative metabolism of various xenobiotics, including drugs, environmental toxins, and endogenous compounds. FMO1 catalyzes the oxygenation of soft nucleophilic heteroatoms (e.g., nitrogen, sulfur) in substrates, often enhancing their solubility and facilitating excretion. While FMO1 is predominantly expressed in the liver and kidneys of most mammals, its expression varies across species and tissues, influencing metabolic pathways and interindividual differences in drug response.
Recombinant FMO1 protein is produced using biotechnological methods, such as heterologous expression in bacterial (e.g., *E. coli*) or mammalian cell systems (e.g., HEK293. insect cells). This allows for large-scale production of the enzyme with high purity and activity. The recombinant form retains the functional characteristics of native FMO1. including its dependence on NADPH and molecular oxygen for catalytic activity, making it a valuable tool for *in vitro* studies.
Research applications of recombinant FMO1 include drug metabolism studies, toxicology assessments, and investigations into enzyme kinetics or substrate specificity. It is particularly useful for identifying potential drug-drug interactions or predicting metabolic stability during drug development. Additionally, recombinant FMO1 aids in studying genetic polymorphisms that affect enzyme activity, which may explain variability in drug efficacy or adverse effects among individuals.
The production of recombinant FMO1 also supports structural biology efforts, enabling crystallographic or cryo-EM studies to elucidate its mechanism and guide the design of enzyme inhibitors or prodrugs. Overall, recombinant FMO1 serves as a critical resource for advancing pharmaceutical research, personalized medicine, and understanding metabolic diseases linked to FMO dysfunction.
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