Cayman Fgfr1 Extracellular Domain (Human, Recombinant), 100ug

Fibroblast growth factor receptor 1 (FGFR1) is a growth factor receptor with roles in cell migration, differentiation, and survival, as well as apoptosis, chemotaxis, and embryonic development.^1,2 It is composed of an N-terminal extracellular domain, which contains three immunoglobulin-like (Ig-like) domains, including the FGF ligand-binding domain, an acidic box, and a CAM-homology domain, a transmembrane domain, and a C-terminal tyrosine kinase domain. FGFR1 is expressed throughout the pre-differentiated mesenchyme of the cranium, in midfacial mesenchyme, and the endochondral skull base during early embryonic development, and broadly expressed in epithelial, osteogenic, and chondrogenic cell lineages by 10 to 13 weeks gestation.³ Upon ligand binding, FGFR1 dimerizes, resulting in autophosphorylation of the tyrosine kinase domain and activation of various intracellular signaling pathways, including the ERK/MAPK pathway.¹ Mutations in FGFR1 induce various craniofacial dysostosis syndromes, such as Crouzon, Pfeiffer, and Jackson-Weiss syndromes that feature basicranial and midfacial deformities.³ FGFR1 amplifications, translocations, and fusions are associated with lung cancer, 8p11 myeloproliferative syndrome, and glioblastoma multiforme, respectively.⁴ Cayman’s FGFR1 Extracellular Domain (human, recombinant) can be used for enzyme activity assays. This protein consists of 275 amino acids, has a calculated molecular weight of 31 kDa, and a predicted N-terminus of Arg22 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 50-55 kDa due to glycosylation.

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