expression of human erythropoietin protein using a baculovirus

Bombyx mori cell (Bm5) was transfected with circular viral DNA from HyNPV and the baculvirus transfer vector with the cDNA of human Erythropeitin. The recombinant virus obtained was plaque purified and inoculated to early fifth instar larvae of the silkworm. At five days post infection, hemolymph was collected and the activity was measured .The rEPO was expressed successfully and was secreted into hemolymph by signal sequence derived from human EPo gene. The molecular weight of the rEPO in this study was approximately 33 KDa which is in confirmation of wide range of molecular weights existing recombinant erythropoietin.