Date Received: 06-06-2025
Date Published: 13-06-2025
##submissions.doi##: https://doi.org/10.31817/tckhnnvn.2013.11.6.
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Co-expression of Human Interleukin-2 Gene with Chaperone GroESL and Thioredoxin in Escherichia coli BL21 (DE3)
Keywords
Chaperone, expression, interleukin-2, thioredoxin, pelB secret signal
Abstract
Interleukin 2 (IL-2), one of the cytokines plays an important role for the immune response. IL-2 promotes the activation of T cells and so often used in immunotherapy such as kidney epithelial malignant and melanoma cancer. Gene encoding il-2 modified Cys125 to Ser was inserted into pET22b(+) harboring pelB secrete signal for expression in E. coli BL21(DE3) cells. To enhance the correct protein folding and solubility, IL-2 was simultaneously expressed with chaperone GroESL and thioredoxin (Trx). The results indicated that IL-2 proteins co-expressed with GroESL and Trx of 20 kDa were still existed in insoluble form and consisted of the pelB secret signal.
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