The synthetic mammalian GnRH-6 gene was inserted into the expression plasmid pMAL-c2.The recombinant plasmid was transformed into E.coli BL21,where the expression of GnRH-6 gene was induced with IPTG.Amylose resin was used to purify the protein by the affinity chromatograph method.The purified products were analyzed using the SDS-PAGE.The reactiongenicity of fusion protein was identified by indirect ELISA.The results showed that the GnRH-6 gene in fusion with the gene encoding maltose binding protein could be expressed at a high level.The fusion protein could be purified efficiently by affinity chromatograph method.The molecular weight of the fusion protein was equal to that of the theory.the reactiongenicity of fusion protein with GnRH antibody was very high.