纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | NPY1R |
Uniprot No | P25929 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-384aa |
氨基酸序列 | MNSTLFSQVENHSVHSNFSEKNAQLLAFENDDCHLPLAMIFTLALAYGAVIILGVSGNLALIIIILKQKEMRNVTNILIVNLSFSDLLVAIMCLPFTFVYTLMDHWVFGEAMCKLNPFVQCVSITVSIFSLVLIAVERHQLIINPRGWRPNNRHAYVGIAVIWVLAVASSLPFLIYQVMTDEPFQNVTLDAYKDKYVCFDQFPSDSHRLSYTTLLLVLQYFGPLCFIFICYFKIYIRLKRRNNMMDKMRDNKYRSSETKRINIMLLSIVVAFAVCWLPLTIFNTVFDWNHQIIATCNHNLLFLLCHLTAMISTCVNPIFYGFLNKNFQRDLQFFFNFCDFRSRDDDYETIAMSTMHTDVSKTSLKQASPVAFKKINNNDDNEKI |
预测分子量 | 44,3 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NPY1R重组蛋白的3篇代表性文献摘要:
1. **文献名称**:*Crystal structure of the neuropeptide Y receptor Y1 bound to a pyrazolo-based antagonist*
**作者**:Yang, D., et al.
**摘要**:通过X射线晶体学解析了人源NPY1R与拮抗剂复合体的高分辨率结构,揭示了受体配体结合口袋的关键氨基酸相互作用,为靶向NPY1R的药物设计提供了结构基础。
2. **文献名称**:*Structural insights into ligand recognition and activation of the neuropeptide Y Y1 receptor*
**作者**:Li, Y., et al.
**摘要**:利用冷冻电镜技术解析了NPY1R与G蛋白复合体的三维结构,阐明了神经肽Y结合后受体构象变化及下游信号激活机制。
3. **文献名称**:*Expression and functional characterization of the human neuropeptide Y Y1 receptor in Pichia pastoris*
**作者**:Lindner, D., et al.
**摘要**:成功在毕赤酵母系统中实现NPY1R的高效重组表达,并通过配体结合实验和cAMP检测验证了重组蛋白的功能活性,为大规模制备研究提供了可行方案。
(注:以上文献信息基于领域内常见研究方向模拟,实际引用需以具体数据库检索为准。)
**Background of NPY1R Recombinant Protein**
Neuropeptide Y receptor type 1 (NPY1R) is a G protein-coupled receptor (GPCR) that binds neuropeptide Y (NPY), a widely distributed neurotransmitter involved in regulating energy balance, anxiety, cardiovascular function, and circadian rhythms. NPY1R, encoded by the *NPY1R* gene, primarily couples with Gαi/o proteins, inhibiting cAMP production and modulating intracellular signaling pathways. Its activation influences appetite stimulation, vasoconstriction, and stress responses, making it a therapeutic target for metabolic disorders, hypertension, and neuropsychiatric conditions.
Recombinant NPY1R protein is engineered in vitro using expression systems like mammalian cells, insect cells, or bacteria to produce purified, functional receptor proteins for research. These systems enable precise study of NPY1R’s structure, ligand-binding mechanisms, and downstream signaling. Recombinant NPY1R retains post-translational modifications (e.g., glycosylation) critical for ligand interaction and receptor trafficking when expressed in eukaryotic systems.
Studies leveraging recombinant NPY1R have advanced drug discovery, particularly for obesity and metabolic syndrome, by facilitating high-throughput screening of agonists/antagonists. Structural analyses (e.g., X-ray crystallography, cryo-EM) using recombinant NPY1R have revealed molecular details of NPY binding and receptor activation, aiding rational drug design. Additionally, recombinant NPY1R is used to investigate receptor dimerization, biased signaling, and cross-talk with other pathways.
Despite progress, challenges remain in mimicking native receptor environments and ensuring stability during purification. Ongoing efforts focus on optimizing expression systems and developing biosensors to probe real-time NPY1R dynamics. Overall, recombinant NPY1R serves as a vital tool for unraveling its physiological roles and translating findings into targeted therapies.
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