In order to clone and express human cardiac troponin I-C fusion protein in application to the quality control for cTnI detection system, human cardiac troponin I and troponin C cDNAs were amplified from human cardiac using gene-specific primers designed from the published cDNA sequences by the polymerase chain reaction. The full-length of cTnI was linked with TnC by a short DNA sequence coding for 19 neutral amino acid residues. An expression construct for cTnI-C was engineered by inserting the corresponding cDNA into a pET15b plasmid. Then recombinant plasmid was transformed into E.coli BL21(DE3)pLysS cells, and protein expression was induced by isopropyl-β-D-thiogalactopyranoside（IPTG）. Soluable expression of cTnI-C in prokaryotic system was successfully obtained. Fusion protein had an N-terminal His-tag sequence which could be purified by affinity chromatography on a Ni²⁺-Sepharose column. After one step affinity chromatography the fusion protein shows homogeneity as judged by SDS-PAGE. The fusion protein was stable and easy to be purified,could be used as candidate reference material for cTnI detection systems.