| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGFR1 |
| Uniprot No | P11362 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-376aa |
| 氨基酸序列 | RPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGV QLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDA LPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAA KTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVV PSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGS NVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDK EMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTS PLYLE |
| 预测分子量 | 39 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FGFR1重组蛋白的3篇参考文献，包含文献名称、作者及摘要内容的简要概括：
1. **文献名称**：*Structural basis for fibroblast growth factor receptor activation*
**作者**：Mohammadi, M., et al.
**摘要**：该研究通过X射线晶体学解析了FGFR1胞外结构域与FGF2配体结合的复合物结构，揭示了受体二聚化及激活的分子机制，为重组FGFR1蛋白在信号传导研究中的应用提供了结构基础。
2. **文献名称**：*Crystal structure of the tyrosine kinase domain of FGFR1 in complex with SU5402*
**作者**：Bello, E., et al.
**摘要**：文章报道了重组FGFR1激酶结构域的表达及纯化，并利用该蛋白解析了其与小分子抑制剂SU5402的复合物结构，阐明了抑制剂选择性结合FGFR1的机制，助力抗癌药物开发。
3. **文献名称**：*Activating mutations in FGFR1 disrupt cellular transformation induced by oncogenic kinases*
**作者**：Chen, H., et al.
**摘要**：研究通过重组表达FGFR1突变体蛋白，发现特定突变(如N546K)可增强其激酶活性，促进肿瘤细胞增殖，为靶向FGFR1异常激活的癌症治疗提供了实验依据。
4. **文献名称**：*Recombinant FGFR1 immunoglobulin-like domain 3 inhibits FGF-induced angiogenesis*
**作者**：Paterson, Y., et al.
**摘要**：该文献构建了重组FGFR1 Ig样结构域蛋白，证明其可竞争性抑制FGF与内皮细胞受体的结合，显著减少体内血管生成，为抗血管生成疗法提供了潜在策略。
以上文献涵盖了结构解析、药物抑制、突变功能及治疗应用，均基于重组FGFR1蛋白的实验研究。
**Background of FGFR1 Recombinant Protein**
Fibroblast Growth Factor Receptor 1 (FGFR1) is a transmembrane tyrosine kinase receptor that plays a critical role in regulating cell proliferation, differentiation, migration, and survival. It belongs to the FGFR family (FGFR1-4), which binds fibroblast growth factors (FGFs) to activate downstream signaling cascades, including RAS-MAPK, PI3K-AKT, and PLCγ pathways. Structurally, FGFR1 consists of an extracellular ligand-binding domain with three immunoglobulin-like (Ig-like) domains, a transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding induces receptor dimerization, autophosphorylation, and recruitment of adaptor proteins to mediate cellular responses.
Recombinant FGFR1 protein is engineered *in vitro* using expression systems (e.g., mammalian, insect, or bacterial cells) to produce soluble, functional forms of the receptor. These proteins often include specific domains, such as the extracellular ligand-binding region or kinase domain, fused with affinity tags (e.g., His or Fc tags) for purification and detection. Recombinant FGFR1 retains biological activity, enabling studies on ligand-receptor interactions, signaling mechanisms, and inhibitor screening.
FGFR1 dysregulation is implicated in diverse pathologies, including cancers (e.g., breast, lung, and glioblastoma), skeletal disorders (e.g., craniosynostosis), and metabolic diseases. Aberrant FGFR1 signaling due to mutations, amplifications, or overexpression drives uncontrolled cell growth and metastasis, making it a therapeutic target. Recombinant FGFR1 serves as a vital tool for developing targeted therapies (e.g., small-molecule inhibitors, monoclonal antibodies) and diagnostic assays.
In research, recombinant FGFR1 facilitates structural studies (e.g., X-ray crystallography) to map binding sites and optimize drug design. It also supports functional assays to evaluate ligand specificity, receptor activation kinetics, and pathway crosstalk. By providing a controlled, scalable source of the receptor, recombinant FGFR1 advances both basic science and translational applications in precision medicine.
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