| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AGRP |
| Uniprot No | O00253 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-132aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMAQMGLAPMEGIRRPDQALLPELPGL GLRAPLKKTTAEQAEEDLLQEAQALAEVLDLQDREPRSSRRCVRLHESCL GQQVPCCDPCATCYCRFFNAFCYCRKLGTAMNPCSRT |
| 预测分子量 | 15 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AGRP重组蛋白的3条代表性文献信息(内容为模拟概括，非真实文献)：
1. **《重组AGRP蛋白在大肠杆菌中的表达与功能鉴定》**
- 作者：Smith, J.R. et al.
- 摘要：研究通过大肠杆菌系统成功表达并纯化重组AGRP蛋白，验证其与黑皮质素受体MC4R的结合活性，证实重组蛋白在抑制α-MSH信号通路中的功能。
2. **《AGRP的核磁共振结构解析及其受体相互作用研究》**
- 作者：Kim, H. & Cone, R.D.
- 摘要：利用NMR技术解析重组AGRP蛋白的三维结构，揭示其C端结构域在竞争性拮抗MC4R中的关键作用，为肥胖治疗靶点提供结构基础。
3. **《重组AGRP片段对食欲调控的动物模型验证》**
- 作者：Fan, W. et al.
- 摘要：通过注射重组AGRP蛋白片段到小鼠下丘脑，观察到显著促进摄食行为和体重增加，证明其在能量平衡调控中的生理重要性。
Agouti-related protein (AGRP) is a neuropeptide predominantly expressed in the hypothalamus, where it plays a central role in regulating energy homeostasis and feeding behavior. As an endogenous antagonist of melanocortin receptors (MC3R and MC4R), AGRP competes with α-melanocyte-stimulating hormone (α-MSH) to inhibit receptor signaling. This pathway is critical for integrating metabolic signals, including leptin and insulin, to modulate appetite and energy expenditure. Dysregulation of AGRP expression or function has been linked to obesity, hyperphagia, and metabolic disorders, making it a key target for studying obesity-related mechanisms.
Recombinant AGRP (rAGRP) is engineered using biotechnological platforms, such as Escherichia coli or mammalian expression systems, to produce purified, bioactive forms of the protein. The recombinant approach ensures high consistency, scalability, and customization (e.g., tagging for detection or affinity purification). rAGRP retains the functional cysteine-rich C-terminal domain necessary for receptor binding, enabling its use in structural studies, receptor interaction assays, and behavioral research. It has been instrumental in elucidating the molecular basis of appetite regulation, including how AGRP neurons integrate hormonal and nutrient signals to drive hunger. Additionally, rAGRP serves as a tool to model metabolic dysfunction in vitro or in animal studies, aiding drug discovery efforts targeting melanocortin pathways. Recent advances also explore its potential in designing therapeutics that modulate MC receptor activity to treat obesity or cachexia. Despite its physiological complexity, rAGRP provides a controlled means to dissect the interplay between neural circuits, metabolism, and disease.
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