Objective:To generate an anti-Met single-chain antibody fragment(scFv)and human IgG Fc fusion protein and increase the solubility of the scFv. Methods:The human IgG Fc gene was amplified by RT-PCR and cloned into the expression vector of pBAD-scFv which had been constructed previously. The anti-Met scFv-Fc expressing vector was transferred into E.coli. Top10 and the fusion protein expression was induced by L-arabinose.The soluble protein was purified by His-affinity chromatography and characterized by SDS-PAGE and Western blot. The specificity of the scFv-Fc fusion protein was confirmed by ELISA. Results:DNA sequence result showed that the cloned scFv-Fc gene sequence was correct, corresponding to the data of GenBank. SDS-PAGE and Western blot showed that the molecular weight of the fusion protein was about 60 ku.The ELISA results confirmed the scFv-Fc fusion protein could bind to Met protein specifically. Conclusion:The solubilty of scFv-Fc fusion protein was increased when compared with that of the scFv fragment.