| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DAO |
| Uniprot No | P14920 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-347aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMRVVVIGAGVIGLSTALCIHERYHSVLQPL DIKVYADRFTPLTTTDVAAGLWQPYLSDPNNPQEADWSQQTFDYLLSHVH SPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPRELDMFPDYGY GWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYII PGTQTVTLGGIFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERT GFRPVRPQIRLEREQLRTGPSNTEVIHNYGHGGYGLTIHWGCALEAAKLF GRILEEKKLSRMPPSHL |
| 预测分子量 | 42 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DAO(D-氨基酸氧化酶)重组蛋白的模拟参考文献示例，内容基于典型研究方向虚构，仅供参考：
1. **文献名称**: *"High-Yield Expression and Purification of Recombinant Human D-Amino Acid Oxidase in Escherichia coli"*
**作者**: Smith J, et al.
**摘要**: 研究通过大肠杆菌表达系统高效制备重组人源DAO蛋白，优化了诱导条件与纯化步骤，验证了其催化D-丝氨酸的活性，为后续酶动力学研究提供基础。
2. **文献名称**: *"Structural Insights into the Substrate Specificity of Recombinant D-Amino Acid Oxidase"*
**作者**: Tanaka K, et al.
**摘要**: 利用X射线晶体学解析重组DAO的三维结构，结合突变实验揭示了其底物结合口袋的关键氨基酸残基，阐明了其对不同D-氨基酸的选择性催化机制。
3. **文献名称**: *"Recombinant DAO Enzyme Delivery for Schizophrenia Model Intervention"*
**作者**: Lee H, et al.
**摘要**: 开发基于纳米载体的重组DAO递送系统，在动物模型中验证其降低脑内D-丝氨酸水平的能力，探讨其在精神分裂症治疗中的潜在应用。
4. **文献名称**: *"Functional Stability of Recombinant DAO under Physiological Conditions"*
**作者**: García-Ruiz P, et al.
**摘要**: 评估重组DAO在不同pH、温度及抑制剂存在下的稳定性，发现其半衰期在生理环境下显著延长，为开发长效DAO疗法提供依据。
注：以上文献为示例性内容，实际研究中请通过PubMed、Google Scholar等平台检索真实论文。
**Background of Recombinant DAO Protein**
D-amino acid oxidase (DAO) is a flavin-dependent enzyme that catalyzes the oxidative deamination of D-amino acids, producing hydrogen peroxide and corresponding α-keto acids. Initially identified in eukaryotic organisms, DAO plays critical roles in regulating neurotransmitter levels (e.g., D-serine, a co-agonist of NMDA receptors) and detoxifying non-canonical amino acids. Its dysfunction is linked to neurological disorders, cancer, and aging-related conditions, driving interest in therapeutic applications.
Traditional DAO extraction from native sources faced challenges like low yield and purity. Advances in recombinant DNA technology enabled the production of recombinant DAO proteins through heterologous expression in microbial systems (e.g., *E. coli*, yeast) or mammalian cell cultures. This approach ensures scalable, cost-effective production with enhanced enzymatic stability and activity.
Recombinant DAO has garnered attention for biomedical and industrial uses. In therapeutics, it is explored for degrading D-serine in schizophrenia or targeting D-amino acids in tumors. Industrially, it serves in biosensors, biocatalysis for chiral compound synthesis, and antibiotic production. Recent engineering efforts, such as rational design and directed evolution, further optimize its substrate specificity, thermostability, and resistance to oxidative inactivation.
Despite progress, challenges remain, including immunogenicity in clinical applications and balancing catalytic efficiency with stability. Ongoing research focuses on structural analysis, fusion protein strategies, and delivery systems to maximize its potential. Recombinant DAO exemplifies the synergy between enzyme engineering and biotechnology, offering versatile solutions for health and industry.
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