The tegumental membrane of platyhelminth parasites is of crucial importance for modulation of the host response and parasite survival. A complementary deoxyribonucleic acid (cDNA) containing an open reading frame of 390 bp, which encodes a profilin-like tegumental protein with a theoretical isoelectric point of 6.02 and a molecular weight of 14.42 kDa, had been identified by bioinformatic analysis. The coding region of the cDNA was cloned into the prokaryotic expression vector pGEX-4T-1 and expressed in Escherichia coli. The purified recombinant protein named rSj15 was immunogenic and could elicit a high titer of antibody in mice. Western blot analysis revealed that the protein was differentially expressed during the different growth stages of Schistosoma japonicum. Immunohistochemical analysis localized the protein to the tegument and underlying tissue of the S. japonicum adult worm. The rSj15 could induce the expressions of IL-12 in the cultured mouse dendritic cell.