Cayman FGFR3 Extracellular Domain (human, recombinant)

Fibroblast growth factor receptor 3 (FGFR3) is a growth factor receptor with roles in early mammalian skeletal development and post-embryonic linear bone growth.¹ It is composed of an N-terminal extracellular domain, which contains three immunoglobulin-like (Ig-like) domains and includes the FGF ligand-binding domain, an acidic box, and a CAM-homology domain, a transmembrane domain, and a C-terminal tyrosine kinase domain.² FGFR3 is broadly expressed in the midfacial mesenchyme and basicranial and paranasal cartilage during embryonic development but is only expressed in the perichondrium and proliferating zone chondrocytes by 10 to 13 weeks gestation.³ Upon ligand binding, FGFR3 dimerizes resulting in autophosphorylation of the tyrosine kinase domain and activation of various intracellular signaling pathways, including the ERK/MAPK pathway.⁴ Gain-of-function mutations in FGFR3 induce achondroplasia, the most common form of dwarfism in humans.¹ Mutations in FGFR3 also induce Muenke syndrome, a craniosynostosis with features including hearing loss, carpal and tarsal anomalies, and behavioral and developmental deficits.⁵ Cayman’s FGFR3 Extracellular Domain (human, recombinant) protein consists of 364 amino acids, has a calculated molecular weight of 39.6 kDa, and a predicted N-terminus of Glu23 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 64.3 kDa due to glycosylation.

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