Expression and Purification of Interferon-τ in Escherichia coli

Objective To express and purify IFN-τ from E.coli. Methods IFN-τ was expressed at 42℃ in recombinant E.coli containing pBV220-IFN-τ vector. The expression product was purified and renaturated by the inclusion body dissolution DEAE ion exchange chromatography ammonium sulfate precipitation and gradient dialysis. Results IFN-τ was highly expressed in E.coli with a molecular size of 21 000 as shown in SDS-PAGE analysis. After purification and renaturation the protein reached a purity of 90%. Conclusion Stable and overexpressive IFN-τcan be achieved by using pBV220-IFN-τ expression system. The expressed IFN-τ can be easily, rapidly and effectively purified by ammonium sulfate precipitation combined with DEAE ion exchange chromatography.