کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8419732 | 1545744 | 2010 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Expression, purification and characterization of recombinant interleukin-21
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوتکنولوژی یا زیستفناوری
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چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Immunological Methods - Volume 362, Issues 1â2, 31 October 2010, Pages 185-189
Journal: Journal of Immunological Methods - Volume 362, Issues 1â2, 31 October 2010, Pages 185-189
نویسندگان
Carol M.Y. Lee, Helen McGuire, Antony Basten, Cecile King, Daniel Christ,