Objective:To express in Pichia pastoris and purify recombinant human osteoprogerin(OPG) fragment OPG179 and human serum albumin(HSA) fusion protein.Methods:The gene of OPG179 was amplified by RT-PCR.The plasmid of pHILD2-rhOPG179-HSA was constructed and then transformed to Pichia pastoris.The rhOPG179-HSA fusion protein was expressed,purified,and analyzed with SDS-PAGE and Western blot.Results:The expression plasmid of pHILD2-rhOPG179-HSA was proved correct after the plasmid was identified and sequenced.The molecular mass of fusion protein was about 97 kD.The rhOPG179-HSA fusion protein was expressed and purified successfully from Pichia pastoris with relative higher-efficient expression level(about 80 mg/L).Conclusion:The secreted recombinant fusion protein rhOPG179-HSA has been successfully expressed and purified,and supply for a foundation for its biological activity analysis.