To　prepare　human　APOBEC3G　and　to　produce　its　antibodies,　the　total　RNA　was　extracted　from　H9　cells,　and　APOBEC3G　gene　was　achieved　by　RT-PCR.　The　resulting　DNA　construct　was　cloned　into　a　prokaryotic　expression　vector　(pET-32a)　and　recombinant　pET-APOBEC3G　was　expressed　in　Eserichia　coli　BL21(DE3)　as　an　insoluble　protein.　The　vector　also　contained　a　six-histidine　(His6)　tag　at　the　C-terminus　for　convenient　purification　and　detection.　To　express　and　purify　the　APOBEC3G　in　E.coli　cells,　the　accuracy　of　inserted　genes　and　specificity　of　APOBEC3G　proteins　were　detected　by　two　enzymes　digestion　technology,　SDS-PAGE,　and　Western　Blot　(WB).　Rabbits　were　immuzied　by　purified　APOBEC3G　proteins.　Serum　samples　were　tested　by　indirect　enzyme-linked　immunosorbent　assays　(ELISAs)　to　determine　the　level　of　antibodies.　The　purity　of　APOBEC3G　was　above　80　%.　The　titer　of　the　antibodies　was　1:102400.