| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | F2RL1 |
| Uniprot No | P55085 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-397aa |
| 氨基酸序列 | MRSPSAAWLLGAAILLAASLSCSGTIQGTNRSSKGRSLIGKVDGTSHVTGKGVTVETVFSVDEFSASVLTGKLTTVFLPIVYTIVFVVGLPSNGMALWVFLFRTKKKHPAVIYMANLALADLLSVIWFPLKIAYHIHGNNWIYGEALCNVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMGHSRKKANIAIGISLAIWLLILLVTIPLYVVKQTIFIPALNITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRMLRSSAMDENSEKKRKRAIKLIVTVLAMYLICFTPSNLLLVVHYFLIKSQGQSHVYALYIVALCLSTLNSCIDPFVYYFVSHDFRDHAKNALLCRSVRTVKQMQVSLTSKKHSRKSSSYSSSSTTVKTSY |
| 分子量 | 44.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下为3篇关于重组人F2RL1(PAR2)蛋白的模拟参考文献示例：
1. **文献名称**：Structural insights into recombinant human protease-activated receptor 2 (PAR2) signaling mechanism
**作者**：Zhang Y, et al.
**摘要**：通过X射线晶体学解析了重组人F2RL1蛋白胞外域与激动剂肽的复合物结构，揭示了PAR2激活过程中的构象变化及关键配体结合位点。
2. **文献名称**：Functional characterization of recombinant PAR2 in inflammatory pain models
**作者**：Smith JL, et al.
**摘要**：利用哺乳动物细胞表达系统制备高纯度重组人F2RL1蛋白，体外实验证实其参与TLR4/NF-κB信号通路交叉对话，并通过小鼠足底注射模型验证其在炎症性疼痛中的调节作用。
3. **文献名称**：Development of a recombinant PAR2-targeted fluorescent probe for cancer imaging
**作者**：Kim S, et al.
**摘要**：基于人源重组F2RL1蛋白设计特异性多肽探针，实现体外结肠癌细胞系高灵敏度荧光标记，为PAR2高表达肿瘤的靶向诊疗提供新工具。
注：以上文献信息为模拟生成，供学术写作格式参考。实际引用需以真实文献为准。
Recombinant human F2RL1 protein, also known as protease-activated receptor 2 (PAR2), is a member of the G protein-coupled receptor (GPCR) family. It plays a critical role in cellular signaling pathways, particularly those involving inflammation, tissue repair, and pain modulation. PAR2 is activated through proteolytic cleavage of its N-terminal domain by serine proteases (e.g., trypsin, mast cell tryptase) or specific synthetic peptides, exposing a tethered ligand that binds intramolecularly to initiate downstream signaling. This receptor is widely expressed in epithelial, endothelial, immune, and neuronal cells, linking extracellular proteolytic activity to intracellular responses such as calcium mobilization, MAPK activation, and NF-κB pathway regulation.
Dysregulation of PAR2 has been implicated in pathological conditions, including chronic inflammation, cancer progression, neurodegenerative diseases, and metabolic disorders. Its dual role in pro- and anti-inflammatory responses makes it a complex therapeutic target. Recombinant F2RL1 proteins, typically produced in mammalian or insect expression systems, retain post-translational modifications essential for ligand binding and signaling. These proteins are vital tools for studying PAR2 activation mechanisms, ligand-receptor interactions, and screening modulators in drug discovery. Recent research focuses on developing PAR2 antagonists or biased agonists to selectively modulate pathways linked to disease, highlighting its potential in precision medicine.
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