To get a large quantity of human glucagon-like peptide-1, different hGLP-1 multimers containing different copies of rhGLP-1 were constructed. The synthetic hGLP-1 cDNA gene was inserted into pET-32a(+) to get the recombinant plasmid pET32-GLP-1, which could express a fusion protein including thioredoxin， hexahistidine, and rhGLP-1. The coding sequence for the fusion protein was repeatedly inserted into the vector in tandem to get pET32-GLP-1-2 and pET32-GLP-1-3 with two or three copies, respectively. Three different plasmids were transformed into E.coli BLR (DE3) and induced by IPTG. The results demonstrated that the three kinds of E.colicells expressed the desired protein and the percentages of the desired protein increased with the numbers of gene copy. The purified rhGLP-1 showed obvious biological activity of lowering plasma glucose.