| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DDO |
| Uniprot No | Q99489 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-341aa |
| 氨基酸序列 | MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGWQIFQS TPTEEVPFWA DVVLGFRKMT EAELKKFPQY VFGQAFTTLK CECPAYLPWL EKRIKGSGGW TLTRRIEDLW ELHPSFDIVV NCSGLGSRQL AGDSKIFPVR GQVLQVQAPW VEHFIRDGSG LTYIYPGTSH VTLGGTRQKG DWNLSPDAEN SREILSRCCA LEPSLHGACN IREKVGLRPY RPGVRLQTEL LARDGQRLPV VHHYGHGSGG ISVHWGTALE AARLVSECVH ALRTPIPKSN L |
| 预测分子量 | 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DDO(D-氨基酸氧化酶)重组蛋白的虚构参考文献示例，涵盖不同研究方向：
1. **《重组D-氨基酸氧化酶在大肠杆菌中的高效表达及活性分析》**
- 作者：Smith J, et al.
- 摘要：研究通过优化大肠杆菌表达系统，成功实现DDO的高效可溶性表达，酶活性达120 U/mg，为工业化生产奠定基础。
2. **《DDO重组蛋白的底物特异性与酶动力学研究》**
- 作者：Zhang L, et al.
- 摘要：系统分析DDO对多种D-氨基酸的催化效率，发现其对D-丝氨酸的Km值为0.5 mM，揭示其在神经信号调控中的潜在作用。
3. **《基于DDO重组蛋白的固定化酶制备及其稳定性提升》**
- 作者：Wang Y, et al.
- 摘要：开发纳米材料固定化DDO技术，使酶在60℃下的半衰期延长至48小时，显著提升工业应用可行性。
4. **《DDO基因沉默对精神分裂症模型小鼠行为学的影响》**
- 作者：Tanaka K, et al.
- 摘要：利用重组DDO调控脑内D-丝氨酸水平，证实其通过NMDA受体途径改善小鼠认知障碍，为靶向治疗提供依据。
注：以上文献为示例性内容，实际研究中建议通过学术数据库(如PubMed、CNKI)检索真实文献。
**Background of DDO Recombinant Protein**
DDO (D-amino acid oxidase) recombinant protein is a genetically engineered enzyme derived from the native D-amino acid oxidase, which plays a critical role in the metabolism of D-amino acids—noncanonical stereoisomers of amino acids. Naturally occurring in organisms ranging from microorganisms to mammals, DDO catalyzes the oxidative deamination of D-amino acids, producing hydrogen peroxide and corresponding α-keto acids. This reaction is vital for regulating D-amino acid levels, particularly in the brain, where D-serine and D-aspartate act as neuromodulators in neurotransmission and synaptic plasticity.
The recombinant form of DDO is produced via heterologous expression systems, such as *E. coli* or yeast, enabling scalable and high-purity protein production. Its recombinant design often incorporates modifications to enhance stability, solubility, or catalytic efficiency, making it a valuable tool for industrial and research applications. In biotechnology, DDO recombinant protein is utilized in biosensors, biocatalysis for chiral compound synthesis, and enzymatic assays to quantify D-amino acids.
In biomedical research, DDO has garnered attention for its potential role in neurodegenerative diseases. Abnormal D-amino acid levels are linked to conditions like schizophrenia, Alzheimer’s, and amyotrophic lateral sclerosis (ALS). Recombinant DDO facilitates studies on D-serine metabolism, aiding drug discovery targeting the N-methyl-D-aspartate (NMDA) receptor pathway. Additionally, it serves as a model enzyme for investigating oxidative stress mechanisms due to its hydrogen peroxide byproduct.
Overall, DDO recombinant protein bridges fundamental biochemistry with applied sciences, offering insights into cellular metabolism and therapeutic innovation.
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