To reconstitute the lyophilized FGF17, it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions.
FGF-17 is a heparin-binding growth factor that is preferentially expressed in the embryonic brain . It shares a high degree of homology with other members of the FGF family, being 60% identical to FGF-8 and 50% identical to FGF-18 . The human recombinant form of FGF-17 is typically produced in Escherichia coli (E. coli) and is available as a lyophilized powder . This recombinant protein is a single, non-glycosylated polypeptide chain containing 219 amino acids and has a molecular mass of approximately 25.2 kDa .
FGF-17 functions as a ligand for gonadotropin-releasing hormone (GnRH), which plays a role in neuron ontogeny . It is involved in the control of differentiation and proliferation of midline cerebrum cells through temporal and spatial gradients . Additionally, FGF-17 has been implicated in congenital hypogonadotropic hypogonadism (CHH) due to mutations in its gene .
Recombinant FGF-17 is widely used in biomedical research for its ability to stimulate cellular processes such as mitogenesis, differentiation, migration, angiogenesis, and wound healing . It is particularly important for maintaining, expanding, and differentiating various types of cells in culture . For example, FGF-17 is used to study signaling interactions and pathways involved in neuron development and function.