Human thymosin alpha 1 (T α 1) is an important peptide in the development and senescence of immunological competence in human, and many studies have reported the expression of this peptide. In this study, we designed and synthesized the Tα1 gene according to the E. coli codon usage preference and constructed a 6 × T α 1 concatemer. The latter was inserted into an E. coli expression vector pET-22b (+), and transformed into E. coli BL21 (DE3). After induction with IPTG, the concatemer protein was successfully expressed in E. coli then cleaved by hydroxylamine to release the T α 1 monomer. Gly-SDS-PAGE and mass spectrometry confirmed that the recombinant protein was cleaved as intended. The bioactivity of the T α 1 monomer was analyzed by lymphocyte proliferation and by mitochondrial activity in two different tumor cell lines. This study provides a description of the preparation of a bioactive T α 1, which may prove useful in future biomedical research.
Zhou, L., Lai, Z.-T., Lu, M.-K., Gong, X.-G., & Xie, Y. (2008). Expression and Hydroxylamine Cleavage of Thymosin Alpha 1 Concatemer. Journal of Biomedicine and Biotechnology, 2008, 1–8. https://doi.org/10.1155/2008/736060