Superoxide　dismutase　(SOD)　family　is　necessary　to　protect　cells　from　the　toxicity　of　reactive　oxygen　species　produced　during　normal　metabolism.　Among　SODs,　manganese-containing　superoxide　dismutase　(Mn-SOD,　SOD2)　is　the　most　important　one.　The　DNA　fragment　containing　the　full　nucleotide　of　full-length　human　SOD2　was　synthesized　and　inserted　into　the　prokaryotic　expression　vector　pGEX-4T-1　with　tag　GST.　DNA　construct　was　then　transformed　into　Escherichia　coli　BL21　(DE3)　and　expression　was　induced　with　IPTG　at　25℃.　The　recombinant　fusion　protein　GST-SOD2　(46　kDa)　was　purified　from　the　bacterial　lysate　by　GST　resin　column　affinity　chromatography.　GST　tag　was　cleaved　with　thrombin,　and　a　crude　SOD2　recombinant　protein　(25　kDa)　was　obtained　and　further　purified　by　heparin　affinity　chromatography.　Activities　of　the　two　SOD2　proteins　were　1788　and　2000　U/mg,　respectively.　Both　SOD2　proteins　were　stable　under　physiological　condition　and　cell-penetrating　(P＜0.05).　Our　findings　open　the　possibility　to　study　the　structure　and　effects　of　two　full-length　recombinant　SOD2　proteins.　©　2017,　Science　Press.　All　right　reserved.