Objective： To express and purify bioactive recombinant human fibroblast growth factor-20 （rhFGF-20）protein and to prepare its polyclonal antisera. Methods： FGF 20 cDNA was amplified from human prostate tissue by RT-PCR and was subcloned into expression vector pET-24a, which was then transformed into the E. coli DE3. Expression of rhFGF-20 protein was induced in E. coli DE3 and the protein was purified by Ni2＋-NTA His-Bind Resins. The purity and biological activity of rh FGF-20 protein were determined by SDS-PAGE and cell-proliferation assay, respectively. Two New Zealand white rabbits were immunized with rhFGF-20 protein to prepare polyclonal antisera and the titer of antibody was determined by double diffusion test. Results： rhFGF-20 protein was efficiently expressed in E. coli DE3 in the form of inclusion body and homogeneous protein was obtained after purification with Ni2-NTA His Bind Resins. Cell proliferation assay indicated that rhFGF-20 dose-dependently （50-5 000 ng/ml） promoted fibroblast cells proliferation. The prepared polyclonal antisera, with a titer of I ： 32, had immunoreatlon with hFGF-20. Conclusion： The expressed rhFGF-20 protein can stimulate the proliferation of fibroblast cells and the prepared antisera are antigen specific