FGF16 Mouse

FGF-16 was initially identified in rat heart tissue through homology-based polymerase chain reaction techniques . The protein is characterized by a core domain of approximately 120 amino acids, which is a common feature among all members of the FGF family. This domain allows for a conserved tertiary structure that is essential for its biological activity.

FGF-16 is a heparin-binding growth factor. Heparin-binding is significant because it enhances the stability and activity of the growth factor. FGF-16 signals through specific fibroblast growth factor receptors (FGFRs), particularly FGFR 2c and 3c . These interactions are crucial for the protein’s role in cellular processes.

FGF-16 has been implicated in several developmental processes. It is involved in the development of the heart and other tissues during embryogenesis. Additionally, FGF-16 has been associated with various diseases. For instance, mutations in the FGF16 gene can lead to conditions such as Metacarpal 4-5 Fusion and Adams-Oliver Syndrome .

Recombinant FGF-16, particularly the mouse variant, is produced using bacterial expression systems such as Escherichia coli. This recombinant protein is used in various research applications to study its biological functions and potential therapeutic uses. The recombinant form retains the biological activity of the native protein, making it a valuable tool for scientific research.

Recombinant FGF-16 is utilized in cell proliferation assays and other functional studies to understand its role in cellular processes. It is also used in studies related to tissue regeneration and repair, given its ability to promote cellular growth and differentiation.