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- W2364884049 abstract "Objective To improve the expression of the soluble recombinant protein of rat IgE-dependent histamine-releasing factor (rHRF) and to optimize the purification procedures by affinity chromatography. Method The complete coding region of rHRF was subcloned into pET-28a vector from the recombinant plasmid pET-30a-rHRF using the multiple cloning sites BamHⅠand XhoⅠ. Recombinant pET-28a-rHRF was then transformed into E.coli BL21 (DE3) cells. Optimal conditions for the expression of the soluble recombinant rHRF were determined by changing the IPTG concentration (0.1～1.0 mmol/L),inducing temperature (25～37℃) and inducing time (1～5 h). The conditions for affinity chromatography were also optimized to improve the purity. Result The recombinant pET-28a-rHRF was constructed successfully. Expression of the soluble recombinant protein was not affected by the IPTG concentration,inducing temperature and the induction time. Compared with the pET-30a-rHRF transformed cells,recombinant proteins expressed by pET-28a-rHRF transformed cells,due to the presence of 6×his tags at the N and C terminus,could be easily purified by the affinity chromatography. Conclusion The expression of the soluble recombinant rHRF was not influenced by the concentration of IPTG,inducing temperature and time. The presence of 6×his tag would greatly facilitate the purification and the subsequence study of the biological functions of rHRF." @default.
- W2364884049 created "2016-06-24" @default.
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- W2364884049 date "2008-01-01" @default.
- W2364884049 modified "2023-09-23" @default.
- W2364884049 title "Optimization of the Expression and Purification of Recombinant Rat IgE-Dependent Histamine-Releasing Factor" @default.
- W2364884049 hasPublicationYear "2008" @default.
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