| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FFAR1 |
| Uniprot No | O14842 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-300aa |
| 氨基酸序列 | MDLPPQLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSLVYALNLGCSDLLLTVSLPLKAVEALASGAWPLPASLCPVFAVAHFFPLYAGGGFLAALSAGRYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLEAPGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCYVGCLRALARSGLTHRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGLKTVCAARTQGGKSQK |
| 预测分子量 | 31,4 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FFAR1(GPR40)重组蛋白的假设性参考文献示例，供参考(建议通过学术数据库核实具体文献)：
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1. **文献名称**: *Structural insights into ligand recognition and activation of FFAR1*
**作者**: Zhang Y. et al. (2021)
**摘要**: 通过冷冻电镜解析人源FFAR1重组蛋白与内源性脂肪酸配体的复合物结构，揭示其跨膜结构域动态激活机制，为靶向药物设计提供依据。
2. **文献名称**: *Functional characterization of recombinant FFAR1 in insulin secretion*
**作者**: Nakamura S. et al. (2019)
**摘要**: 在HEK293细胞中重组表达FFAR1.证实其介导长链脂肪酸增强葡萄糖依赖性胰岛素分泌的功能，并筛选出小分子激动剂TUG-424的协同作用。
3. **文献名称**: *Optimization of FFAR1 recombinant expression in E. coli for high-throughput screening*
**作者**: Wang L. et al. (2020)
**摘要**: 开发大肠杆菌系统中FFAR1跨膜结构域的可溶性重组表达与纯化策略，用于基于结构的虚拟药物筛选平台构建。
4. **文献名称**: *FFAR1 agonists improve glucose tolerance via biased signaling pathways*
**作者**: Hauge M. et al. (2017)
**摘要**: 利用重组FFAR1蛋白结合β-arrestin招募实验，发现部分激动剂通过偏向性信号通路调控胰岛素分泌，减少传统通路副作用。
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**注意**：以上为模拟文献，实际研究中建议通过PubMed、Web of Science等平台检索关键词(如FFAR1 recombinant、GPR40 structure/agonist)获取真实文献。
FFAR1 (Free Fatty Acid Receptor 1), also known as GPR40. is a class A G protein-coupled receptor (GPCR) that plays a critical role in regulating metabolic homeostasis. It is primarily expressed in pancreatic β-cells, enteroendocrine cells, and specific regions of the brain. FFAR1 is activated by medium- to long-chain free fatty acids (FFAs), which bind to its extracellular domain, triggering intracellular signaling pathways. Upon activation, FFAR1 couples with Gαq/11 proteins, leading to the stimulation of phospholipase C (PLC), calcium mobilization, and subsequent potentiation of glucose-stimulated insulin secretion (GSIS). This mechanism positions FFAR1 as a key therapeutic target for type 2 diabetes mellitus (T2DM), as enhancing insulin release in a glucose-dependent manner could mitigate hyperglycemia without risking hypoglycemia.
Recombinant FFAR1 proteins are engineered versions of the receptor, typically produced in heterologous expression systems such as mammalian cells (HEK293. CHO), insect cells, or yeast. These systems enable large-scale production of functional, purified FFAR1 for structural and functional studies. Recombinant FFAR1 retains ligand-binding specificity and signaling properties, making it invaluable for drug discovery, ligand screening, and mechanistic studies. Structural analyses (e.g., X-ray crystallography, cryo-EM) using recombinant FFAR1 have revealed key details about its ligand-binding pocket and activation mechanisms, guiding the design of synthetic agonists. Notably, compounds like TAK-875 (fasiglifam) were developed to target FFAR1. though clinical trials highlighted challenges such as hepatotoxicity.
Current research focuses on optimizing FFAR1 modulators for safety and efficacy, leveraging recombinant protein tools to explore biased signaling and allosteric regulation. These efforts underscore FFAR1's potential as a druggable target for metabolic disorders.
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