Purification and characterization of prokaryotically expressed human interferon-lambda2
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1Allergy and Inflammation Research Institute, Shantou University Medical College, Shantou, Guangdong, PR China. mingcai_li@yahoo.com
Abstract:
A system for the production of soluble interferon (IFN)-lambda2 was developed by fusing the IFN-lambda2, NusA protein, polyhistidine and S peptide genes and then expressing the fused product (Nus-His-S-tagged IFN-lambda2) in Escherichia coli. The expressed fusion protein was purified by Ni-NTA affinity chromatography. The fusion tag was removed from recombinant IFN-lambda2 by cleavage with enterokinase. N-Terminal sequencing confirmed the identity of the purified protein. When compared with commercial IFN-alpha2b, IFN-lambda2 had similar antiviral activity. The production and characterization of biologically active IFN-lambda2 will be beneficial for its potential role in clinical applications.
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