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- W2364595087 abstract "Objective To optimized expression conditions of human mBAFF by using recombinant vector pQE80L-mBAFF,and Escherichia coli DH5α.Methods The effects of inducing time,IPTG concentration,and temperature on mBAFF expression were assayed.After optimization of expression conditions,mBAFF were expressed and the proteins were purified by Ni~(2+)-NTA chromatography and SepharcryL S200 chromatography.The binding activity of mBAFF to cell was assayed by flow cytometry;the biological activity of mBAFF was detected by MTT assay.Results Optimum inducing time,temperature,IPTG concentration for mBAFF expression were found,which were(4 h),37 ℃,and 0.2 mmol/L,respectivelg.The mBAFF protein is about 35% of total protein of the host.After purification,the purity of the expressed protein reached above 98%.The mutant protein ccould bind the surface receptors of lymphocytes but could not stimulate proliferation of lymphocytes.Conclusion Optimum conditions for mBAFF protein expression are obtained,which provides a basis for gene engineering technology." @default.
- W2364595087 created "2016-06-24" @default.
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- W2364595087 date "2006-01-01" @default.
- W2364595087 modified "2023-09-27" @default.
- W2364595087 title "Soluble expression of human mBAFF in Escherichia coli and its characterization" @default.
- W2364595087 hasPublicationYear "2006" @default.
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