In this study, we propose a strategy for recombinant protein expression under conditions of low temperatures. The low-temperature production of recombinant proteins was conducted in a cell-free protein synthesis reaction through the fusion of the N-terminus of the protein of interest with that from a temperature-insensitive protein. For instance, while the expression of hlL-2 or $TNF-{alpha}$ was negligible when the reaction temperature was below $20^{circ}C$, fusion constructs of the N-terminus of these proteins with the N-terminus of CAT allowed for a substantial expression of the fused protein. This method is predicted to provide a useful approach for the expression of unstable and/or aggregation-prone protein.