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Expression,purification,and characterization of a functional mutant recombinant human interleukin-2
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نویسنده
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liu m. ,wang b. ,sun g. ,qian d. ,yan z. ,song x. ,ding s.
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منبع
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protein and peptide letters - 2010 - دوره : 17 - شماره : 10 - صفحه:1280 -1284
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چکیده
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In the current study,a mutant recombinant human interleukin-2 (mhil-2) was generated using site-directed mutagenesis. the bacteria transformed with plasmid pet15b-mhil-2 were cultured in lb medium containing 0.6mm iptg for 8 hours at 27°c. approximately 90% of his-mhil-2 was efficiently expressed in soluble form. purification efficiency was optimized using a number of strategies,including nickel ion chelating chromatography,desalting chromatography,thrombin cleavage and superdex 75 gel filtration chromatography. the final product had >95% purity. pbmcs,cd4+ and cd8+ t cell proliferation assays revealed that one such mutant has identical functional property to the wildtype hil-2. in summary,we generated a mutant hil-2 that is functionally identical to wild-type hil-2. © 2010 bentham science publishers ltd.
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کلیدواژه
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Biological activity; Chromatography; Expression; Interleukin-2; Mutant; Purification; Soluble form
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آدرس
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clinical immunologic laboratory,hospital of medical college qingdao university,no.16 jiangsu road, China, key laboratory of medicine and biotechnology,qingdao university medical college,no.38 dengzhou road, China, clinical immunologic laboratory,hospital of medical college qingdao university,no.16 jiangsu road, China, key laboratory of medicine and biotechnology,qingdao university medical college,no.38 dengzhou road, China, key laboratory of medicine and biotechnology,qingdao university medical college,no.38 dengzhou road, China, key laboratory of medicine and biotechnology,qingdao university medical college,no.38 dengzhou road, China, key laboratory of medicine and biotechnology,qingdao university medical college,no.38 dengzhou road, China
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Authors
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