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- W1967288946 endingPage "714" @default.
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- W1967288946 abstract "The chemokines eotaxin-1 (CCL11) and eotaxin-2 (CCL24), belonging to the CC chemokines family, play key roles in the inflammatory response, allergic asthma and other diseases. When expressed in Escherichia coli, chemokines are prone to form inclusion bodies devoid of biological activity, and it is hard to refold them properly. Here an expression and purification protocol for high-level production of soluble and biologically active CCL11 and CCL24 in E. coli has been established. A final yield of 8.7 mg/l for CCL11 and 3.9 mg/l for CCL24 has been obtained and the purified proteins were characterized with SDS-PAGE, mass spectrometry and circular dichroism. High binding affinity of purified chemokines with CC chemokine receptor type 3 (CCR3) has been confirmed with surface plasmon resonance (SPR) and the KD values are 3.7 × 10−7 M and 3.0 × 10−7 M, respectively, for CCL11 and CCL24. This report provides a straightforward strategy for the efficient production of soluble and biologically active chemokines in E. coli." @default.
- W1967288946 created "2016-06-24" @default.
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- W1967288946 creator A5076731987 @default.
- W1967288946 date "2014-04-01" @default.
- W1967288946 modified "2023-09-24" @default.
- W1967288946 title "High-level production of biologically active chemokines in Escherichia coli" @default.
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- W1967288946 doi "https://doi.org/10.1016/j.procbio.2014.01.021" @default.
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