Fusion expression of human thymosin alpha 1 in Escherichia coli.
- Author:
Zhao-Yang XIU
1
;
Ying YU
;
Chang-Qing CHEN
Author Information
1. Research Center of Biotechnology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, Shanghai 200233, China.
- Publication Type:Journal Article
- MeSH:
Escherichia coli;
genetics;
Genetic Engineering;
Humans;
Recombinant Fusion Proteins;
biosynthesis;
isolation & purification;
Thymosin;
analogs & derivatives;
biosynthesis;
genetics;
isolation & purification
- From:
Chinese Journal of Biotechnology
2002;18(5):541-545
- CountryChina
- Language:Chinese
-
Abstract:
Engineering E. coli strain, BL21 (DE3)/pGEX-4T-human Thymosin alpha 1, was constructed by oligonucleotide annealing and PCR amplifying the target gene, then ligating it with pGEX-4T-3 vector and transferring into BL21 host. The yield of fusion protein of GST-Thymosin alpha 1 expressed from BL21 (DE3)/pGEX-4T-thymosin alpha 1 is about 35%-40% of total protein after fermentation. Following the simple cut of thrombin or CNBr, about 0.2 g/L thymosin alpha 1 can be harvested. The product is checked by MS and activity test, which indicates that the recombinant product has full biological activity of native thymosin alpha 1.
