Background: The fibroblast growth factor (FGF) family is essential to tissue development
and stem cell differentiation; therefore, there is increasing interest in the clinical application
of FGFs, resulting in increasing demand for active recombinant human FGFs (rhFGFs).
Objective: To improve the production of rhFGF18, we determined the optimal culture conditions
required to maximize rhFGF18 protein expression in E. coli
Method: Competent cell type, inducer concentration, induction temperature, and induction time
for the optimal expression of rhFGF18 were analysed.
Results: The rhFGF18 protein expression was highest in BL21 competent cells at an L-arabinose
induction concentration of 0.1% (w/v), an induction temperature of 10 °C, and an induction time
of 6 h under the control of an araBAD promoter introduced using the pBAD-HisA vector.
Conclusion: Under optimal culture conditions, the rhFGF18 protein could induce osteogenic differentiation
by increasing the alkaline phosphatase activity and mineralization activity. The approaches
described herein may be useful for producing active rhFGF18 to meet the increasing
demands for its pharmacological application, allowing for its future clinical use.