| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MAOB |
| Uniprot No | P27338 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-489aa |
| 氨基酸序列 | SNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSV |
| 预测分子量 | 59.3kDa |
| 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MAOB重组蛋白的3篇参考文献示例(文献信息为示例，非真实存在)：
1. **《High-yield Expression and Purification of Human MAOB in E. coli for Enzymatic Studies》**
- 作者：Smith, J. et al. (2019)
- 摘要：该研究报道了利用大肠杆菌表达系统高效表达人源MAOB重组蛋白，通过优化诱导条件和亲和层析纯化，获得高活性蛋白，并分析了其底物特异性及酶动力学参数，为药物筛选提供了基础。
2. **《Crystal Structure of Recombinant MAOB Complexed with a Selective Inhibitor》**
- 作者：Zhang, L. et al. (2020)
- 摘要：研究团队采用杆状病毒-昆虫细胞系统表达MAOB，通过X射线晶体学解析了MAOB与选择性抑制剂的复合物结构，揭示了抑制剂结合位点的关键氨基酸残基，为靶向药物设计提供了结构依据。
3. **《Functional Characterization of MAOB Expressed in Yeast: Role in Neurodegenerative Disease Models》**
- 作者：Lee, S. et al. (2021)
- 摘要：本文利用毕赤酵母系统表达重组MAOB，验证其在体外对多巴胺的代谢活性，并证明其在帕金森病细胞模型中调节氧化应激的作用，提示其作为治疗靶点的潜力。
**注意**：以上文献为示例，实际研究中请通过PubMed、Web of Science等数据库检索真实文献。
Monoamine oxidase B (MAO-B) is a mitochondrial outer membrane-bound enzyme that plays a critical role in the metabolism of monoamine neurotransmitters, including dopamine, phenethylamine, and benzylamine. It catalyzes the oxidative deamination of these substrates, producing hydrogen peroxide and aldehydes as byproducts. Dysregulation of MAO-B activity has been implicated in neurodegenerative disorders like Parkinson's disease, psychiatric conditions, and cancer progression. Recombinant MAO-B protein, produced through heterologous expression systems (e.g., E. coli, insect, or mammalian cells), enables detailed biochemical and structural studies of this flavin adenine dinucleotide (FAD)-dependent enzyme.
The recombinant form retains catalytic activity and dimeric structure, mimicking native MAO-B properties. Its production allows standardized investigation of enzyme kinetics, substrate specificity, and inhibitor interactions. MAO-B inhibitors (e.g., selegiline, rasagiline) developed using recombinant protein screening are clinically used to enhance dopaminergic signaling in Parkinson's disease. Recent research also explores MAO-B's role in cellular oxidative stress and apoptosis regulation, linking it to Alzheimer's pathology and glioblastoma.
Advantages of recombinant MAO-B include batch consistency, scalability, and elimination of tissue-source variability. Structural studies using recombinant protein have revealed substrate/inhibitor binding sites and mechanisms of FAD cofactor interaction, informing drug design. However, challenges persist in mimicking post-translational modifications critical for membrane association. Current applications span drug discovery, diagnostic tool development, and mechanistic studies of neurotoxicity. MAO-B remains a key therapeutic target, with recombinant protein technology accelerating translational research in neurology and oncology.
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