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Expression, purification and characterization of recombinant interleukin-21


Interleukin-21 (IL-21) is a key regulator of the immune system. However, studies of this cytokine have so far been hampered by the limited availability of recombinant protein preparations. Here we describe a method based on refolding of inclusion bodies expressed in E. coli by rapid dilution. The method was applied to human and murine IL-21 proteins, which were further purified by affinity chromatography and gel-filtration. The proteins are pure and highly active as determined by endotoxin and cell proliferation assays. The availability of milligram quantities of protein enabled us to generate monoclonal antibody fragments against the cytokine and will aid in further structural, biochemical and physiological analyses.

Type Journal
ISBN 1872-7905 (Electronic) 0022-1759 (Linking)
Authors Lee, C. M.; McGuire, H.; Basten, A.; King, C.; Christ, D.;
Published Date 2010-10-01
Published Volume 362
Published Issue 1-2
Published Pages 185-9
Status Published in-print
URL link to publisher's version
OpenAccess link to author's accepted manuscript version