| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DA |
| Uniprot No | Q8TAP4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-145aa |
| 氨基酸序列 | MLSVQPDTKP KGCAGCNRKI KDRYLLKALD KYWHEDCLKC ACCDCRLGEV GSTLYTKANL ILCRRDYLRL FGVTGNCAAC SKLIPAFEMV MRAKDNVYHL DCFACQLCNQ RFCVGDKFFL KNNMILCQTD YEEGLMKEGY APQVR |
| 预测分子量 | 16,5 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DA重组蛋白的示例参考文献(注：以下内容为模拟生成，实际文献请通过学术数据库查询)：
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1. **文献名称**: *Expression and Purification of Recombinant Dopamine D2 Receptor in E. coli*
**作者**: Zhang, L., et al.
**摘要**: 本研究报道了利用大肠杆菌表达系统高效表达人源多巴胺D2受体(DA-D2R)的重组蛋白。通过优化密码子及纯化步骤，获得了高纯度蛋白，为后续受体功能研究提供了材料基础。
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2. **文献名称**: *Structural Insights into DA-binding Proteins via Cryo-EM*
**作者**: Thompson, R.J., & Kim, S.
**摘要**: 利用冷冻电镜技术解析了DA重组蛋白(DA-RP1)与配体的复合物三维结构，揭示了其特异性结合位点及构象变化机制，为靶向药物设计提供了结构依据。
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3. **文献名称**: *Recombinant DA Protein Alleviates Parkinsonian Symptoms in Rodent Models*
**作者**: Gupta, A., et al.
**摘要**: 实验证明，重组表达的多巴胺能蛋白(DA-Protein X)可通过血脑屏障并在帕金森病模型小鼠中显著改善运动功能障碍，提示其潜在治疗价值。
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4. **文献名称**: *Optimization of Yeast-based Production for DA Fusion Proteins*
**作者**: Müller, F., & Schmidt, H.
**摘要**: 通过改造毕赤酵母表达系统，实现了DA重组融合蛋白(DA-FP2)的高效分泌表达，产量较传统方法提升3倍，降低了工业化生产成本。
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**提示**：实际研究中建议通过PubMed、Web of Science等平台，以关键词“recombinant dopamine protein”“DA receptor expression”等检索最新文献。
**Background of Recombinant Proteins**
Recombinant proteins are engineered molecules produced through genetic engineering techniques, enabling the synthesis of specific proteins by introducing exogenous DNA into host organisms. This technology emerged in the 1970s with advancements in molecular cloning, revolutionizing biotechnology by allowing large-scale production of proteins that are otherwise scarce or difficult to isolate from natural sources.
The process involves inserting a target gene into expression vectors (e.g., plasmids), which are then introduced into host cells such as *E. coli*, yeast, insect, or mammalian cells. These hosts utilize their cellular machinery to transcribe and translate the gene into the desired protein. Prokaryotic systems like *E. coli* are favored for simplicity and cost-effectiveness, while eukaryotic systems (e.g., CHO cells) are used for complex proteins requiring post-translational modifications (e.g., glycosylation).
Recombinant proteins have transformative applications across medicine, research, and industry. Therapeutically, they are pivotal in producing insulin, monoclonal antibodies, vaccines (e.g., hepatitis B), and cytokines (e.g., interferons). In research, they serve as tools for studying protein functions, drug screening, and structural biology. Industrially, they are used in enzymes for biofuels, food processing, and bioremediation.
Challenges include optimizing expression yields, ensuring proper protein folding, and minimizing host-induced modifications. Innovations like CRISPR-Cas9. cell-free systems, and synthetic biology continue to refine production efficiency and expand possibilities. Recombinant protein technology remains a cornerstone of modern biotechnology, driving advancements in personalized medicine, sustainable manufacturing, and scientific discovery.
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