We performed Differential Display techniques to search genes involved in the phenotypic alteration present in these gestational trophoblastic tumors. This strategy resulted in the isolation of one transcript upregulated in choriocarcinoma JEG-3 .cell line, called GTT1. This cDNA encodes a protein of 295 amino acid residues, containing a conserved START domain involved in lipid transport. Here, we report the cDNA cloning of GTT1 into the high-expression vector pRSET-B. Expression of this plasmid in Escherichia coli BL21 (DE3) resulted in the overproduction of the recombinant protein. The presence of a histidine tag in the expressed protein allowed us a very fast purification through one-step affinity chromatography on nickel-charged beads, the yield of purified protein was ~ 24mg per Iiter of culture. In addition, immunization of rabbits with the recombinant protein produced antitibodies that were able to recognize GTT1 protein. Both recombinant protein and its specific antibodies will allow to study the functional role of GTT1/StarD7 in lipid signaling mediated cellular events.