FGF 2 Human, sf9

FGF-b is a single, glycosylated polypeptide chain consisting of 155 amino acids and has a molecular mass of approximately 17.353 kDa . The sequence of the first five N-terminal amino acids is Ala-Ala-Gly-Ser-Ile . The protein is produced in Sf9 insect cells using a baculovirus expression system .

FGF-b is a heparin-binding growth factor that stimulates the proliferation of a variety of cell types, including mesenchymal, neuroectodermal, and endothelial cells . It also exerts potent angiogenic activity in vivo, promoting the formation of new blood vessels . The biological activity of FGF-b is measured by its ability to induce the proliferation of BAF3 cells expressing FGF receptors, with an ED50 of less than 0.5 ng/ml, corresponding to a specific activity of 2 million units per milligram .

The recombinant FGF-b is purified using proprietary chromatographic techniques to achieve a purity greater than 98%, as determined by reverse-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) . The protein is typically formulated as a sterile, filtered liquid solution containing 20 mM Tris (pH 7.9), 100 mM KCl, 1 mM DTT, and 20% glycerol .

FGF-b is stable at 4°C for up to three weeks but should be stored desiccated below -18°C for long-term storage . To prevent degradation, it is recommended to add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) and to avoid multiple freeze-thaw cycles .

FGF-b is widely used in laboratory research for studying cell proliferation, differentiation, and angiogenesis. It is also used in tissue engineering and regenerative medicine due to its ability to promote cell growth and tissue repair .

In summary, Fibroblast Growth Factor-Basic (Human Recombinant, Sf9) is a crucial protein in biological research and medical applications, offering significant potential for advancing our understanding of cell biology and developing new therapeutic strategies.