Arabidopsis thaliana sterol glycosyltransferase (SGT), UGT80A2, was expressed from stably transformed Drosophila melanogaster Schneider 2 (S2) cells. Recombinant SGT was detected in both intracellular and extracellular fractions with a molecular mass of approximately 76 kDa. Secreted recombinant SGT accounted for approximately 60% of the total recombinant SGT production. Recombinant SGT in the extracellular fractions was purified to homogeneity using a simple one-step Ni-NTA affinity fractionation. Radiometrical assay using uridine diphospho-D-[U-$^{14}C$]glucose (UDP-$^{14}C$-glucose) as a sugar donor and sterols, ${eta}$-sitosterol and stigmasterol, as sugar acceptors showed that the purified recombinant SGT contained UDP-glycosyltransferase activity and could attach $^{14}C$-glucose to ${eta}$-sitosterol and stigmasterol. Recombinant SGT contained higher catalytic activity with ${eta}$-sitosterol, which was similar to the recombinant SGT produced by a bacterial expression system. The transfer of $^{14}C$-glucose by recombinant SGT was further determined by gas chromatography-mass spectrometry (GC-MS) analysis of cellulase-treated $^{14}C$-glucose-transferred ${eta}$-sitosterol and stigmasterol reactants.