| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FMO5 |
| Uniprot No | P49326 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-533aa |
| 氨基酸序列 | MTKKRIAVIGGGVSGLSSIKCCVEEGLEPVCFERTDDIGGLWRFQENPEEGRASIYKSVIINTSKEMMCFSDYPIPDHYPNFMHNAQVLEYFRMYAKEFDLLKYIRFKTTVCSVKKQPDFATSGQWEVVTESEGKKEMNVFDGVMVCTGHHTNAHLPLESFPGIEKFKGQYFHSRDYKNPEGFTGKRVIIIGIGNSGGDLAVEISQTAKQVFLSTRRGAWILNRVGDYGYPADVLFSSRLTHFIWKICGQSLANKYLEKKINQRFDHEMFGLKPKHRALSQHPTLNDDLPNRIISGLVKVKGNVKEFTETAAIFEDGSREDDIDAVIFATGYSFDFPFLEDSVKVVKNKISLYKKVFPPNLERPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKTLPSQSEMMAEISKAQEEIDKRYVESQRHTIQGDYIDTMEELADLVGVRPNLLSLAFTDPKLALHLLLGPCTPIHYRVQGPGKWDGARKAILTTDDRIRKPLMTRVVERSSSMTSTMTIGKFMLALAFFAIIIAYF |
| 分子量 | 73.2 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人FMO5蛋白的3篇参考文献及其摘要概括：
1. **"Structural and Functional Characterization of Human Flavin-Containing Monooxygenase 5 (FMO5)"**
*Authors: Zhang J, Cashman JR*
摘要：该研究通过重组表达人FMO5蛋白，解析其晶体结构并揭示其独特的底物结合口袋特征，发现其对长链脂肪酸的氧化活性，提示其在脂代谢中的潜在作用。
2. **"Substrate Specificity of Recombinant Human FMO5 and its Role in Drug Metabolism"**
*Authors: Hines RN, Koukouritaki SB*
摘要：研究利用重组人FMO5在哺乳动物细胞中的表达，系统评估其对多种药物及内源性化合物的催化活性，发现其对硫醚类化合物的独特氧化偏好性，拓展了FMO5在药物代谢中的功能认知。
3. **"Recombinant Human FMO5 Exhibits Distinct Biophysical Properties and Bile Acid-Modifying Activity"**
*Authors: Shimizu M, Hiroya K*
摘要：通过大肠杆菌重组表达人FMO5.首次证明该酶对初级胆汁酸的化学修饰能力，提出其在肠道菌群-宿主共代谢中的新功能，为代谢疾病研究提供新方向。
Flavin-containing monooxygenase 5 (FMO5) is a member of the FMO enzyme family, which plays a critical role in the oxidative metabolism of various xenobiotics, including therapeutic drugs, dietary compounds, and environmental toxins. As a flavin-dependent enzyme, FMO5 catalyzes the oxygenation of nucleophilic heteroatoms (e.g., nitrogen, sulfur) in substrates, contributing to detoxification and metabolic pathways. Unlike other FMO isoforms (e.g., FMO1-4), FMO5 exhibits distinct substrate specificity and tissue expression patterns, with high levels detected in the liver, kidney, and gastrointestinal tract.
Recombinant human FMO5 protein is produced using heterologous expression systems (e.g., *E. coli*, mammalian cells) to enable functional and structural studies. Its production facilitates research into enzymatic mechanisms, substrate interactions, and regulatory roles in metabolic homeostasis. Studies suggest FMO5 may influence lipid metabolism and aging-related pathways, potentially linking it to metabolic disorders like obesity and diabetes.
The recombinant protein is vital for *in vitro* assays, drug metabolism studies, and toxicity screening, helping predict drug-drug interactions and optimize pharmacokinetics. Additionally, it aids in exploring FMO5’s physiological roles beyond xenobiotic metabolism, such as modulating bile acid synthesis or oxidative stress responses. Despite progress, the full scope of FMO5’s biological functions remains under investigation, highlighting the importance of accessible recombinant tools for advancing biomedical and pharmaceutical research.
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