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- W2004409178 abstract "Human thymosin alpha 1 (T<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>α</mml:mi></mml:math>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<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mrow><mml:mi>T</mml:mi><mml:mi>α</mml:mi><mml:mn>1</mml:mn></mml:mrow></mml:math>gene according to the E. coli codon usage preference and constructed a 6<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mo>×</mml:mo></mml:math>T<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>α</mml:mi></mml:math>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<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>α</mml:mi></mml:math>1 monomer. Gly-SDS-PAGE and mass spectrometry confirmed that the recombinant protein was cleaved as intended. The bioactivity of the T<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>α</mml:mi></mml:math>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<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>α</mml:mi></mml:math>1, which may prove useful in future biomedical research." @default.
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- W2004409178 date "2008-01-01" @default.
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- W2004409178 title "Expression and Hydroxylamine Cleavage of Thymosin Alpha 1 Concatemer" @default.
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- W2004409178 doi "https://doi.org/10.1155/2008/736060" @default.
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