The signal peptide cleavage of Cyprinus carpio var. jian LEP-A1 (jlLEP-A1) and LEP-B (jlLEP-B) sites were identified by SignalP-4.0 software. And pairs of primers were designed to amplify the jlleptiA1 and jlleptinB ORF region without the signal peptide sequence. The amplification products were ligated into the prokaryotic expression vector of pET-32a (+) and pGex-4T-1 respectively, and the recombination plasmida were constructed. The plasmid sequence was confirmed by sequencing and transferred into the host bacteria, Escherichia coli BL21 (DE3). The recombinant proteins of pET-32a(+)/jlLEP-A1, pET-32a(+)/jlLEP-B, pGex-4T-1/jlLEP-A1 and pGex-4T-1/jlLEP-B were highly expressed by induction with IPTG. The optimum concentration of IPTG was 1 mmol/L for 5 h at 37℃. The recombinant proteins mainly existed in soluble form as revealed by SDS-PAGE electrophoresis analysis. The results provided useful information for research on jlleptin function.