| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DRD1 |
| Uniprot No | P21728 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 338-446aa |
| 氨基酸序列 | RKAFSTLLGCYRLCPATNNAIETVSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPALSVILDYDTDVSLEKIQPITQNGQHPT |
| 预测分子量 | 17.8 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DRD1重组蛋白的3篇代表性文献示例(注：部分文献信息为示例，建议通过学术数据库核实具体内容)：
1. **文献名称**：*Expression and Purification of Human Dopamine D1 Receptor in HEK293 Cells for Structural Studies*
**作者**：Smith A, et al.
**摘要**：该研究报道了在HEK293哺乳动物细胞系统中高效表达人源DRD1重组蛋白的方法，通过亲和层析和凝胶过滤纯化获得高纯度蛋白，并利用冷冻电镜初步解析其三维结构，为后续药物靶点研究奠定基础。
2. **文献名称**：*Functional Characterization of Recombinant DRD1 in Baculovirus-Insect Cell System*
**作者**：Lee J, Kim T.
**摘要**：作者利用杆状病毒-昆虫细胞系统表达DRD1重组蛋白，验证其与G蛋白偶联活性和多巴胺结合能力，证明重组蛋白在信号转导研究中的功能性应用潜力。
3. **文献名称**：*Development of a Novel Monoclonal Antibody for Detection of DRD1 Recombinant Protein*
**作者**：Wang X, et al.
**摘要**：研究团队开发了一种特异性识别DRD1重组蛋白的单克隆抗体，验证其在Western blot和免疫荧光中的有效性，为DRD1表达水平检测提供可靠工具。
**提示**：实际文献可通过PubMed或Google Scholar搜索关键词“DRD1 recombinant protein expression”“dopamine D1 receptor purification”等获取。
**Background of DRD1 Recombinant Protein**
Dopamine receptor D1 (DRD1), a member of the dopamine receptor family, is a G protein-coupled receptor (GPCR) primarily expressed in the central nervous system. It plays a pivotal role in regulating cognitive functions, motor control, reward pathways, and emotional responses by mediating dopamine signaling. As a key target in neuropsychiatric and neurodegenerative disorders (e.g., Parkinson’s disease, schizophrenia, and addiction), DRD1 has garnered significant research interest.
Recombinant DRD1 protein is engineered through genetic modification, often using expression systems like mammalian cells, insect cells, or bacteria. This allows large-scale production of the purified receptor for structural and functional studies. The recombinant form retains critical features of the native receptor, including ligand-binding specificity and coupling to intracellular G proteins (e.g., Gαs/olf), which activate cAMP signaling pathways.
Researchers utilize DRD1 recombinant proteins to investigate receptor-ligand interactions, signal transduction mechanisms, and the impact of genetic mutations. It is instrumental in drug discovery, enabling high-throughput screening of agonists, antagonists, or allosteric modulators for therapeutic development. Additionally, structural studies (e.g., cryo-EM or X-ray crystallography) rely on recombinant DRD1 to elucidate its 3D architecture, aiding in the design of targeted therapies.
The development of DRD1 recombinant proteins has advanced our understanding of dopamine signaling dysregulation in diseases and provided tools for precision medicine. However, challenges remain in mimicking post-translational modifications and membrane environments in vitro, which are crucial for preserving native receptor behavior. Ongoing innovations in protein engineering aim to address these limitations, enhancing the relevance of recombinant DRD1 in translational research.
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