OBJECTIVE To induce the expression of and purify invasion plasmid antigen C (IpaC) of Shigella flexneri for studying the pathogenesis of Shigella flexneri. METHODS Prokaryotic expression plasmid pET32a-ipaC was constructed and incorporated into E.coli BL21 (lambda DE3). The engineered bacteria were induced by isopropyl-beta-D-thiogalactopyranoside (IPTG) to express IpaC, which was identified by SDS-PAGE and purified by QIA expressionist system. RESULTS SDS-PAGE presented a band for the fusion protein with the relative molecular mass of approximately 63 000, whose expression reached up to 11% of the total protein of E.coli BL21(lambda DE3). After proper purification, a purity of the target fusion protein of over 90% was achieved when the concentration of imidazole for elution was 350 mmol/L. CONCLUSIONS The recombinant plasmid pET32a-ipaC has been stably and efficiently expressed in E.coli BL21 (lambda DE3), and QIA expressionist purification system proves to be simple and highly efficient.