The human recombinant FGF-a is produced in Sf9 insect cells using a baculovirus expression system. This method results in a single, glycosylated polypeptide chain containing 140 amino acids and having a molecular mass of approximately 15,803 Daltons . The protein is purified using proprietary chromatographic techniques to ensure high purity and biological activity .
The recombinant FGF-a is typically provided as a sterile, filtered liquid formulation. The formulation contains:
The protein solution is stable when stored at 4°C for short-term use (2-4 weeks) and at -20°C for long-term storage. It is recommended to add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) to prevent multiple freeze-thaw cycles .
FGF-a functions as a modifier of endothelial cell migration and proliferation, acting as an angiogenic factor. It is a potent mitogen for various mesoderm- and neuroectoderm-derived cells in vitro, suggesting its involvement in organogenesis . The biological activity of FGF-a is measured by its ability to stimulate the proliferation of BAF3 cells expressing FGF receptors, with an effective dose (ED50) of less than 10 ng/ml, corresponding to a specific activity of 100,000 IU/mg .
Due to its significant role in cell growth and development, FGF-a is widely used in laboratory research. It is particularly valuable in studies related to: