Recombinant FGFR4 protein (His tag)

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Recombinant Human FGFR4 (Fibroblast Growth Factor Receptor 4) fragment (amino acids 44-369) is a high-purity protein designed for studying receptor function and signaling. This fragment includes the Ig-like C2-type 2 and Ig-like C2-type 3 domains, making it an ideal tool for investigating domain-specific interactions, ligand binding, and structural studies in cell proliferation, differentiation, and metabolic regulation research.

Fibroblast Growth Factor Receptor 4 (FGFR4) is a tyrosine-protein kinase that serves as a cell-surface receptor for fibroblast growth factors, playing critical roles in regulating cell proliferation, differentiation, migration, and metabolic processes including lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism, and phosphate homeostasis. It mediates key signaling pathways through phosphorylation of downstream targets like PLCG1 and FRS2, activating RAS/MAPK and AKT1 pathways. FGFR4 is primarily localized to the cell membrane as a single-pass type I membrane protein but undergoes internalization to endosomes and recycling back to the membrane, with isoform 2 being secreted. Mutations leading to constitutive activation or impaired inactivation result in aberrant signaling, underscoring its importance in cellular regulation and disease mechanisms.