| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGFR2 |
| Uniprot No | P21802-20 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 285-704aa |
| 氨基酸序列 | RMKNTTKKPDFSSQPAVHKLTKRIPLRRQVSAESSSSMNSNTPLVRITTR LSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEA VGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINL LGACTQDGPLYVIFEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTF KDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARD INNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLG GSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTF KQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSP DPMPYEPCLPQYPHINGSVKT |
| 预测分子量 | 74 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. |
1. **《Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome》**
作者：Yun Chen, Xianyang Li, Thomas A. Einhorn
摘要：该研究通过重组FGFR2蛋白的晶体结构解析，揭示了FGFR2在Apert综合征相关突变中的异常激活机制，为理解受体二聚化及信号传导异常提供结构基础。
2. **《Recombinant FGFR2 extracellular domain ameliorates lung fibrosis by antagonizing fibroblast growth factor signaling in mice》**
作者：Kazuhisa Nakayama, Hiroyuki Iwamoto
摘要：利用重组FGFR2胞外域蛋白阻断异常FGF信号通路，在小鼠模型中显著减轻肺纤维化，证明其作为潜在治疗策略的有效性。
3. **《Targeting FGFR2 in gastric cancer: Development of a recombinant protein-based high-throughput screening assay》**
作者：Sara M. Johnson, Robert L. Hudkins
摘要：开发基于重组FGFR2蛋白的高通量筛选平台，用于发现新型小分子抑制剂，为胃癌靶向治疗提供先导化合物筛选工具。
4. **《Functional characterization of FGFR2 mutations in craniosynostosis using recombinant receptor proteins》**
作者：Emily R. Parker, Michael J. Dixon
摘要：通过重组FGFR2突变体蛋白的功能分析，揭示了颅缝早闭症相关突变导致受体组成性激活的分子机制，为精准治疗奠定基础。
Fibroblast Growth Factor Receptor 2 (FGFR2) 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 pathways, including RAS-MAPK, PI3K-AKT, and PLCγ. FGFR2 is essential for embryonic development, particularly in skeletal formation, tissue repair, and organogenesis. Structurally, it consists of an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyrosine kinase domain. Alternative splicing generates two major isoforms: FGFR2-IIIb (epithelial) and FGFR2-IIIc (mesenchymal), which exhibit distinct ligand-binding specificities and tissue expression patterns.
Recombinant FGFR2 proteins are engineered in vitro to study its biochemical properties, signaling mechanisms, and interactions with therapeutic agents. These proteins are typically produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, such as glycosylation, which is crucial for ligand binding and receptor activation. Purification methods often involve affinity chromatography (e.g., His-tag or Fc-fusion tags) to achieve high purity. Recombinant FGFR2 is widely used in drug discovery to screen inhibitors targeting FGFR2 dysregulation, which is implicated in cancers (e.g., gastric, breast, and endometrial cancers) and genetic disorders like craniosynostosis syndromes. Mutations or amplifications in FGFR2 can lead to constitutive activation, driving oncogenic signaling. Researchers also utilize recombinant FGFR2 to investigate ligand-receptor specificity, receptor dimerization, and downstream pathway modulation. Its applications extend to structural studies (e.g., X-ray crystallography) to resolve binding interfaces and guide rational drug design. Overall, recombinant FGFR2 serves as a vital tool for understanding FGFR biology and developing targeted therapies.
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