Abstract
A fusion thymosin α1-soluble B lymphocyte stimulator (TMα1–cBLyS) gene was generated to engineer a bifunctional lymphokine, which was then over-produced in Escherichia coli. The molecular weight of the expressed fusion protein was approximately 28 kDa. After being purified by Ni-NTA affinity column, the fusion protein had full activity of BLyS with a slightly higher immunological action than synthetic TMα1. Because TMα1 regulates the cellular immune response and cBLyS amplifies the humoral response, this bifunctional lymphokine could be useful in the treatment of various immunodeficiency syndromes and serve as an immunomodulator to enhance the host’s response to vaccination.
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Revisions requested 15 October 2004; Revisions received 26 November 2004;
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Shen, Q., Tian, R., Ma, W. et al. Construction and expression of a new fusion protein, thymosin α1–cBLyS, E. coli. Biotechnol Lett 27, 143–148 (2005). https://doi.org/10.1007/s10529-004-7333-3
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DOI: https://doi.org/10.1007/s10529-004-7333-3