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Overexpression of Soluble Human Thymosin Alpha 1 in Escherichia coli

Pei-FuCHEN、Hong-YingZHANG、Geng-FengFU、Gen-XingXU、Ya-YiHOU

2005生物化学与生物物理学报：英文版Biochemistry, Genetics and Molecular Biology被引 1

摘要

Synthesized gene of human thymosin alpha 1 (Tα1) was inserted into pET-28a, pET-9c,pThioHis B, pGEX-2T or pBV222 and then inductively expressed in strains of Escherichia coll. Among the five expression systems, the BL21/pET-28a system provides the highest expression level of fusion protein in a soluble form, which is up to 70% of total expressed bacterial proteins as visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The resulting fusion protein purified through nickel affinity chromatography accounts for 2.53% of the wet bacterial pellet weight and reaches 94.5% purity by SDS-PAGE. These results indicate the potential of this expression system for high-throughput production of recombinant Tα1.

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