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Journal of Biomedicine and Biotechnology
Volume 2008, Article ID 736060, 8 pages
Research Article

Expression and Hydroxylamine Cleavage of Thymosin Alpha 1 Concatemer

Room 345, College of Life Sciences, Zhejiang University, Hangzhou 310058, China

Received 3 December 2007; Revised 21 February 2008; Accepted 15 June 2008

Academic Editor: Nina Prak

Copyright © 2008 Liang Zhou et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Human thymosin alpha 1 (T 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 gene according to the E. coli codon usage preference and constructed a 6 T 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 1 monomer. Gly-SDS-PAGE and mass spectrometry confirmed that the recombinant protein was cleaved as intended. The bioactivity of the T 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 1, which may prove useful in future biomedical research.