期刊
JOURNAL OF IMMUNOLOGICAL METHODS
卷 362, 期 1-2, 页码 185-189出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jim.2010.08.008
关键词
Protein expression; Protein purification; Interleukin-21; Phage display
资金
- National Health and Medical Research Council
- Cancer Institute NSW
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. call 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. (C) 2010 Elsevier B.V. All rights reserved.
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