Recombinant Human FGFR3 (IIIc)-Fc Chimera (carrier-free)
Description
Fibroblast growth factor receptors (FGFRs) are transmembrane tyrosine kinase receptors that belong to the immunoglobulin (Ig) superfamily and bind to fibroblast growth factors (FGFs). Activation of FGFRs is involved in cell survival, proliferation, migration, and differentiation. There are four human FGFR genes (FGFR1-4). Each FGFR comprises an extracellular ligand binding domain, a single transmembrane domain, and an intracellular tyrosine kinase domain. The extracellular ligand binding domain contains three immunoglobuline-like (Ig-like) loops, a short cluster of conserved acidic amino acids, and a heparin binding domain. The Ig-like loop III is the core of the ligand-binding site. Alternative splicing in Ig-like loop III results in IIIb and IIIc isoforms of FGFR1-3 and changes the receptor specificity. FGFR3 is associated with many cancers and in fact, it is one of the most mutated genes in human cancers. 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. It has been shown that FGFR3 IIIc/FGF18 signaling is required for colorectal cancer growth and migration. FGFR3 IIIc also plays critical roles in bone development and maintenance. FGFR3 IIIc knockout mice exhibit significant skeletal overgrowth and other skeletal abnormalities. Furthermore, gain of function mutations of FGFR3 cause chondrodysplasia syndromes including achondroplasia, hypochondroplasia, and thanatophoric dysplasia.