Expression, Purification, and Characterization of a Functional Mutant Recombinant Human Interleukin-2

Author(s): Mingjun Liu, Bin Wang, Guirong Sun, Dongmeng Qian, Zhiyong Yan, Xuxia Song, Shouyi Ding

Journal Name: Protein & Peptide Letters

Volume 17 , Issue 10 , 2010

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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 wild-type hIL-2. In summary, we generated a mutant hIL-2 that is functionally identical to wild-type hIL-2.

Keywords: Biological activity, chromatography, expression, interleukin-2, mutant, purification, soluble form

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Article Details

Year: 2010
Page: [1280 - 1284]
Pages: 5
DOI: 10.2174/092986610792231474
Price: $65

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