title: Purification and characterization of prokaryotically expressed human interferon-lambda2.
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.
authors.affiliation: Allergy and Inflammation Research Institute, Shantou University Medical College, Shantou, Guangdong, PR China. mingcai_li@yahoo.com
authors.forename: Mingcai
authors.initials: M
authors.lastname: Li
authors.forename: Dongyang
authors.initials: D
authors.lastname: Huang
mesh_terms: D000998:Antiviral Agents / Q000494:pharmacology; D002460:Cell Line; D016207:Cytokines / Q000302:isolation & purification* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004847:Epithelial Cells / Q000187:drug effects; D015870:Gene Expression / Q000187:drug effects; D006801:Humans; D007378:Interleukins / Q000302:isolation & purification* / Q000378:metabolism*; D010957:Plasmids / Q000378:metabolism; D011387:Prokaryotic Cells / Q000187:drug effects / Q000378:metabolism*; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D000095022:Interferon Lambda
chemical_list: D000998:Antiviral Agents; D016207:Cytokines; D007378:Interleukins; D011994:Recombinant Proteins; C000624353:interferon-lambda, human; D000095022:Interferon Lambda