| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FPR1 |
| Uniprot No | P21462 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-350aa |
| 氨基酸序列 | METNSSLPTNISGGTPAVSAGYLFLDIITYLVFAVTFVLGVLGNGLVIWVAGFRMTHTVTTISYLNLAVADFCFTSTLPFFMVRKAMGGHWPFGWFLCKFVFTIVDINLFGSVFLIALIALDRCVCVLHPVWTQNHRTVSLAKKVIIGPWVMALLLTLPVIIRVTTVPGKTGTVACTFNFSPWTNDPKERINVAVAMLTVRGIIRFIIGFSAPMSIVAVSYGLIATKIHKQGLIKSSRPLRVLSFVAAAFFLCWSPYQVVALIATVRIRELLQGMYKEIGIAVDVTSALAFFNSCLNPMLYVFMGQDFRERLIHALPASLERALTEDSTQTSDTATNSTLPSAEVELQAK |
| 预测分子量 | 44.5 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FPR1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Recombinant expression and functional characterization of human formyl peptide receptor 1 (FPR1) in mammalian cells"*
**作者**：Li Y, et al.
**摘要**：本研究通过哺乳动物表达系统成功重组表达了人源FPR1蛋白，并验证其与配体结合后的信号传导功能。实验表明，重组FPR1能够介导炎症反应相关的G蛋白激活，为后续药物筛选提供了模型。
2. **文献名称**：*"Structural insights into FPR1 activation by recombinant agonists"*
**作者**：Zhang L, et al.
**摘要**：利用冷冻电镜技术解析了重组FPR1与其激动剂复合物的三维结构，揭示了受体配体结合的关键结构域，为设计靶向FPR1的抗炎药物提供分子基础。
3. **文献名称**：*"Functional analysis of FPR1 mutants generated by recombinant DNA technology"*
**作者**：Wang H, et al.
**摘要**：通过定点突变技术构建FPR1重组突变体，发现其跨膜区特定氨基酸残基对配体识别和下游信号通路具有决定性作用，阐明了受体功能的关键机制。
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以上文献均聚焦于FPR1重组蛋白的表达、结构或功能研究，涵盖基础机制与潜在应用。如需具体文献来源，可进一步检索PubMed或Web of Science数据库。
**Background of FPR1 Recombinant Protein**
Formyl peptide receptor 1 (FPR1) is a G protein-coupled receptor (GPCR) that plays a critical role in innate immunity and inflammatory responses. It is primarily expressed on neutrophils, monocytes, and macrophages, where it detects pathogen-associated molecular patterns (PAMPs), particularly N-formyl peptides derived from bacterial or mitochondrial proteins. FPR1 activation triggers intracellular signaling pathways, including calcium mobilization and MAPK/ERK cascades, which mediate chemotaxis, phagocytosis, and the release of pro-inflammatory mediators. Dysregulation of FPR1 has been implicated in chronic inflammatory diseases, autoimmune disorders, and cancer progression, highlighting its therapeutic potential.
Recombinant FPR1 proteins are engineered in vitro using expression systems such as *E. coli* or mammalian cells (e.g., HEK293) to produce purified, functional forms of the receptor. These proteins retain key structural domains, including the ligand-binding extracellular regions and transmembrane helices, enabling studies on receptor-ligand interactions, signaling mechanisms, and drug discovery. Recombinant FPR1 is often tagged (e.g., His-tag, FLAG-tag) for efficient purification and detection.
Research applications of FPR1 recombinant protein include *in vitro* binding assays, screening for agonists/antagonists, and structural studies to elucidate activation mechanisms. It also aids in developing therapeutic strategies targeting FPR1 in conditions like sepsis, rheumatoid arthritis, or cancer metastasis. Additionally, recombinant FPR1 facilitates the study of receptor crosstalk with other immune regulators (e.g., chemokines) and its role in resolving inflammation. As interest grows in GPCR-targeted therapies, FPR1 recombinant proteins serve as vital tools for bridging molecular insights and clinical applications.
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