Apolipoprotein A-I (apoA-I) is the major protein component of high density lipoproteins. This protein has key functions in lipoprotein metabolism and its plasma concentration is inversely correlated with the incidence of atherosclerosis and cardiovascular diseases. There is an increasing need to develop methods for efficient production of recombinant apoA-I for using it in basic research or pharmacological therapy. An apoA-I variant lacking two amino acid residues at the N-terminus can be easily produced by bacterial expression. We report here the characterization of this variant comparing its properties with those of the protein isolated from human serum. The results validate the use of this variant in future assays and investigations.