Objective： To express and purify of human scFv antibody（C1） against the asialoglycoprotein receptor fused to enhanced green fluorecsent protein, and observe its binding capacity to HepG2. Methods：The recombinant plasmid EGFPC1／pET-26b proved by DNA sequencing was transformed into E. coli BL21, and induced for fusion expression of EGFPC1with IPTG, the green fluorescence of E.coli BL21 harboring plasmid EGFPC1／pET-26b was observed under the fluorecsent microscope. The expressed EGFPC1 was purified with Ni2+ chelating HiTrap HP column, and detected with SDS-PAGE. HepG2 was incubated with the recombinant EGFPC1, and the binding bioactivity was observed under the fluorecsent microscope. Results：The green fluorescence of E. coli BL21 harboring plasmid GFPS1／pET-26b was catched under the fluorecsent microscope. The recombinant GFPS1 protein was expressed in E.coli as inclusion body, rGFPS1 was prepared with Ni2+ column purification. The result of immunofluorecsent detection verified that scFv C1 could specificially bind membrane of HepG2 cells. Conclusion：The purified EGFPC1 has strong binding capacity to the membrane of HepG2 using EGFP as a labeling protein, indicated the scFv C1 has a potential value as a targeting molecule for biological therapy of hepatoma; The constructed EGFP／pET-26b can also be used for research of other targeting molecule.