FGF6 Human

FGF-6 is structurally related to other members of the FGF family, especially FGF-4 . It is a cytokine that binds preferentially to two specific FGF receptors: FGFR1 and FGFR4 . The human recombinant form of FGF-6 is typically expressed in Escherichia coli and purified to high levels of purity for research purposes .

FGF-6 plays a crucial role in muscle regeneration. It is involved in the proliferation and migration of myoblasts (muscle precursor cells) and their differentiation into mature muscle fibers . The activity of FGF-6 is dose-dependent, meaning that its effects vary with concentration. At high concentrations, FGF-6 up-regulates FGFR1, which promotes cell proliferation, and down-regulates FGFR4, which promotes cell differentiation .

In addition to its role in muscle tissue, FGF-6 may also act as a regulator of bone metabolism . This dual functionality makes it a valuable protein for studying muscle and bone-related diseases and conditions.

The recombinant form of FGF-6 is produced using bacterial expression systems, such as E. coli. The protein is expressed with an N-terminal methionine and purified to a high degree of purity, often exceeding 95% as analyzed by SDS-PAGE and HPLC . The endotoxin levels are kept very low to ensure the protein’s suitability for research applications .

Recombinant FGF-6 is widely used in laboratory research to study its effects on cell proliferation, differentiation, and migration. It is particularly useful in muscle regeneration studies and has potential applications in developing therapies for muscle-wasting diseases .

For optimal stability, the lyophilized form of recombinant FGF-6 should be stored at temperatures below -70°C. Upon reconstitution, it remains stable for up to one week at 4°C or up to three months at -20°C, provided that a carrier protein, such as bovine serum albumin (BSA), is added to prevent degradation .