Abstract To express the bovine interleukin-18(BoIL-18) protein, cDNA fragment encoding the mature BoIL-18 protein was subcloned into pGEX6p-1 and transformed into E.coli BL21(DE3) . The expressed BoIL-18 protein was purified by affinity Chromatography. MTT method ,ELISA method and VSV were used to assay the functional activity of BoIL-18 protein. Results: The recombinant BoIL-18 was highly expressed in E.coli and purified by affinity Chromatography method. The reBoIL-18 could enhance the proliferation of PBMC, induce IFN-γproducing in spleen lymphocyte. Conclusion: The purified reBoIL-18 has functional activity and can be applied for further studies.
