| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NPY |
| Uniprot No | P01303 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-97aa |
| 氨基酸序列 | MLGNKRLGLSGLTLALSLLVCLGALAEAYPSKPDNPGEDAPAEDMARYYS ALRHYINLITRQRYGKRSSPETLISDLLMRESTENVPRTRLEDPAMW |
| 预测分子量 | 37 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NPY重组蛋白的示例参考文献(注：文献为示例性质，建议通过学术数据库查询真实文献)：
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1. **文献名称**：*High-yield expression and purification of recombinant neuropeptide Y in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：报道了利用大肠杆菌表达系统高效生产重组NPY的方法，采用His标签纯化技术获得高纯度蛋白，并证实其与天然NPY在受体结合实验中活性一致。
2. **文献名称**：*Structural insights into recombinant neuropeptide Y through X-ray crystallography*
**作者**：Jones B, et al.
**摘要**：通过重组表达的人NPY进行结晶和X射线分析，揭示了其与Y1受体结合的关键构象变化，为药物设计提供结构基础。
3. **文献名称**：*Functional modulation of Y2 receptor by site-directed mutagenesis of recombinant NPY*
**作者**：Zhang C, et al.
**摘要**：利用重组NPY突变体研究其与Y2受体的相互作用，发现特定氨基酸残基对信号转导的调控作用。
4. **文献名称**：*Recombinant NPY attenuates anxiety-like behavior in zebrafish models*
**作者**：Brown D, et al.
**摘要**：在小鼠和斑马鱼模型中，注射重组NPY显著降低焦虑样行为，支持其在神经系统疾病中的潜在治疗价值。
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建议通过PubMed、Web of Science等平台以关键词“recombinant NPY”或“neuropeptide Y expression”检索最新研究。
Neuropeptide Y (NPY) recombinant protein is a synthetically produced version of the endogenous NPY, a 36-amino-acid peptide widely distributed in the central and peripheral nervous systems. First identified in 1982. NPY plays critical roles in regulating physiological processes such as appetite, stress response, energy homeostasis, cardiovascular function, and emotional behavior. Its widespread expression and diverse functions make it a key target for studying metabolic disorders, neurological diseases, and cardiovascular conditions.
Structurally, NPY belongs to the pancreatic polypeptide family, characterized by a conserved N-terminal polyproline helix and a C-terminal α-helix stabilized by an amidated tyrosine residue. This unique conformation enables NPY to interact with G protein-coupled receptors (Y1. Y2. Y4. Y5. and y6), triggering intracellular signaling cascades. Recombinant NPY is typically produced using bacterial (e.g., E. coli) or mammalian expression systems, requiring precise post-translational modifications—particularly C-terminal amidation—to maintain bioactivity.
The development of recombinant NPY has addressed challenges associated with isolating the native peptide from biological tissues, enabling standardized research applications. It serves as an essential tool for elucidating NPY receptor interactions, pathway mechanisms, and therapeutic potential. Studies utilizing recombinant NPY have advanced our understanding of its dual role in obesity (stimulating appetite via hypothalamic Y1/Y5 receptors) and neuroprotection (modulating stress responses and neuronal survival). Additionally, it facilitates drug discovery efforts targeting NPY receptors for conditions like anxiety, hypertension, and metabolic syndrome.
Recent advancements in protein engineering have improved the stability and purity of recombinant NPY, supporting both academic research and preclinical development. Its applications extend to in vitro assays, animal model studies, and structural biology investigations, underscoring its versatility as a research reagent and potential therapeutic agent.
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