| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGFRL1 |
| Uniprot No | Q8N441 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-378aa |
| 氨基酸序列 | ARGPPKMADKVVPRQVARLGRTVRLQCPVEGDPPPLTMWTKDGRTIHSGW SRFRVLPQGLKVKQVEREDAGVYVCKATNGFGSLSVNYTLVVLDDISPGK ESLGPDSSSGGQEDPASQQWARPRFTQPSKMRRRVIARPVGSSVRLKCVA SGHPRPDITWMKDDQALTRPEAAEPRKKKWTLSLKNLRPEDSGKYTCRVS NRAGAINATYKVDVIQRTRSKPVLTGTHPVNTTVDFGGTTSFQCKVRSDV KPVIQWLKRVEYGAEGRHNSTIDVGGQKFVVLPTGDVWSRPDGSYLNKLL ITRARQDDAGMYICLGANTMGYSFRSAFLTVLPDPKPPGPPVASSSSATS LPWPVDHHHHHH |
| 预测分子量 | 40 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FGFRL1重组蛋白的3篇示例参考文献(内容为模拟构造，仅供参考)：
1. **文献名称**：*"Recombinant FGFRL1 extracellular domain inhibits FGF signaling in vitro"*
**作者**：Xu, Y. et al.
**摘要**：研究通过大肠杆菌表达系统纯化了FGFRL1的重组胞外结构域蛋白，发现其能够竞争性结合FGF2.抑制经典FGFR1介导的MAPK信号通路，提示FGFRL1可能作为FGF信号的负调控因子。
2. **文献名称**：*"Structural and functional characterization of FGFRL1 reveals its role in skeletal development"*
**作者**：Smith, J.R. & Watanabe, H.
**摘要**：利用重组FGFRL1蛋白进行晶体结构解析，发现其与FGF8具有高亲和力结合能力。动物实验表明，FGFRL1缺失会导致小鼠骨骼发育异常，重组蛋白可部分挽救表型，表明其在骨形成中的关键作用。
3. **文献名称**：*"FGFRL1 recombinant protein suppresses tumor growth by blocking angiogenesis"*
**作者**：Chen, L. et al.
**摘要**：通过哺乳动物细胞表达系统获得高纯度FGFRL1重组蛋白，体内实验证明其通过抑制VEGF和FGF2介导的内皮细胞迁移，显著降低肿瘤血管生成，为癌症治疗提供潜在策略。
(注：以上文献为示例，实际研究需查阅PubMed、Web of Science等数据库获取真实信息。)
Fibroblast Growth Factor Receptor-Like 1 (FGFRL1) is a transmembrane protein belonging to the fibroblast growth factor receptor (FGFR) family. Unlike canonical FGFRs (FGFR1-4), FGFRL1 lacks the intracellular tyrosine kinase domain essential for downstream signaling, suggesting a distinct regulatory role. It is primarily expressed in developing skeletal tissues, kidneys, and muscles, implicating its involvement in organogenesis, bone development, and tissue repair. FGFRL1 interacts with FGF ligands and heparan sulfate proteoglycans, potentially acting as a decoy receptor to modulate FGF signaling pathways by sequestering ligands or forming non-functional complexes with other FGFRs.
Recombinant FGFRL1 protein is engineered to study its structure-function relationships, ligand-binding properties, and therapeutic potential. Produced via mammalian or insect cell expression systems, it retains extracellular domains critical for ligand interaction, such as three immunoglobulin-like (Ig) domains and a conserved acidic box. Purification typically involves affinity chromatography (e.g., His-tag) followed by size-exclusion chromatography to ensure homogeneity. Researchers utilize this protein in vitro to investigate its inhibitory effects on FGF-mediated processes, including cell proliferation, differentiation, and survival. In vivo studies explore its role in skeletal dysplasia, cancer (e.g., lung adenocarcinoma), and kidney diseases, where dysregulated FGF signaling is implicated.
Current research focuses on FGFRL1’s dual role as a tumor suppressor or promoter, depending on context, and its potential as a biomarker or therapeutic target. Challenges include elucidating its precise molecular mechanisms and developing isoform-specific modulators. Recombinant FGFRL1 remains a vital tool for advancing understanding of FGF signaling complexity and its pathophysiological implications.
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