The cDNA of human FGF-21 was subcloned into the pSUMO expression vector and the fusion protein was induced to express in Escherichia coli Rosetta (DE3).  The recombinant hFGF-21 was expressed in soluble form in the pSUMO expression system.  The recombinant fusion protein was purified by Ni-NTA   column.  The purified recombinant protein was dialyzed against PBS for re-nature.  To obtain pure and active recombinant protein, the fusion protein was subjected to cleavage with SUMO protease I.  To examine glucose regulation activity of hFGF-21, 3T3-L1 pre-adipocytes were differentiated into adipocytes, glucose up-take   activity of hFGF-21 was examined by glucose oxidase and peroxidase (GOD-POD) assay.  Compared with no stimulation control, the recombinant hFGF-21 treatment led to a significant increase in glucose consumption of adipocytes and a significant decrease in concentration of glucose in the medium (P < 0.05, P < 0.001).