Fibroblast Growth Factor Receptor 3 (FGFR3) is a member of the fibroblast growth factor receptor family, which plays a crucial role in various cellular processes including cell growth, differentiation, angiogenesis, wound healing, and tumorigenesis . FGFR3 is a transmembrane tyrosine kinase receptor that belongs to the immunoglobulin (Ig) superfamily and binds to fibroblast growth factors (FGFs) . The receptor is involved in cell survival, proliferation, migration, and differentiation .
FGFR3 consists of an extracellular ligand-binding domain, a single transmembrane domain, and an intracellular tyrosine kinase domain . The extracellular domain contains three immunoglobulin-like (Ig-like) loops, a short cluster of conserved acidic amino acids, and a heparin-binding domain . Alternative splicing in the Ig-like loop III results in IIIb and IIIc isoforms of FGFR1-3, which change the receptor specificity . FGFR3 IIIc binds many FGFs including FGF-1, -2, -4, -6, -8, -9, -18, -19, and -20, while FGFR IIIb only binds to FGF-1, -9, and -16 .
The FGFR3 Fc Chimera is a recombinant protein that combines the extracellular domain of FGFR3 with the Fc region of human IgG1 . This fusion protein is designed to enhance the stability and solubility of FGFR3, making it suitable for various research applications . The Fc region also allows for easy purification and detection using Fc-specific antibodies .
The recombinant FGFR3 Fc Chimera is typically produced in mammalian cell lines such as NS0 or 293E cells . The protein is expressed with a linker sequence and a C-terminal human IgG1, resulting in a disulfide-linked homodimer . The recombinant protein is then purified using affinity chromatography and characterized by SDS-PAGE to ensure high purity and correct molecular weight .
FGFR3 Fc Chimera is widely used in research to study the role of FGFR3 in various cellular processes and diseases . It is particularly useful in cancer research, as FGFR3 is one of the most mutated genes in human cancers . The recombinant protein can be used to inhibit FGF-dependent proliferation of cells, making it a valuable tool for studying the signaling pathways involved in cancer and other diseases .