FGF-18 was first identified in 1998, along with FGF-17, as newly discovered murine genes closely related to FGF-8 by sequence homology . These proteins were eventually grouped into the FGF8 subfamily, which includes several endocrine FGF superfamily members such as FGF8, FGF17, and FGF18 .
The recombinant mouse FGF-18 protein is typically produced in various expression systems, such as HEK293 cells or E. coli. The recombinant protein often includes a polyhistidine tag at the C-terminus to facilitate purification . The secreted recombinant mouse FGF-18 comprises 191 amino acids and has a predicted molecular mass of 22.5 kDa. Due to glycosylation, it migrates as an approximately 30-35 kDa band in SDS-PAGE under reducing conditions .
FGF-18 has been shown to play significant roles in various biological processes:
Recombinant mouse FGF-18 is used in various research applications, including studies on cell growth, tissue repair, and developmental biology. The protein is typically lyophilized from sterile PBS and can be stored under sterile conditions at -20°C to -80°C for up to twelve months . It is recommended to aliquot the protein for optimal storage and avoid repeated freeze-thaw cycles .