Abstract: Objective To clone and express Taenia saginata asiatica's Spef1-like gene,and purify its protein.Methods The homologous sequence of adult Taenia saginata asiatica's Spef1-like gene and its full-length coding region were obtained from the full-length eDNA library by PCR and sequenced.Meanwhile the encoding sequence was cloned into the prokaryotic expression vector pET-28a(+).Then it was digested with endonuclease and then expressed in E.coli BL21 with IPTG induction.The recombinant product was purified according to the protocol NTA agarose and detected by SDS-PAGE.Results Spef1-like gene cDNA sequence was obtained and then successfully cloned into pET-28a(+) vector.SDS-PAGE results showed that the gene expression took place in Escherichia coli BL21/DE3,and highly pure protein was achieved.Conclusion Taenia saginata asiatica's Spef1-like gene was successfully cloned and its expression and fusion protein was purified,which provides favorite conditions for further studies of the gene.