expression, production, and renaturation of a functional single-chain variable antibody fragment (scfv) against human icam-1
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ID: 224641
2014
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Abstract
Intercellular adhesion molecule-1 (ICAM-1) is an important factor in the progression of inflammatory responses in vivo. To develop a new anti-inflammatory drug to block the biological activity of ICAM-1, we produced a monoclonal antibody (Ka=4.19×10−8 M) against human ICAM-1. The anti-ICAM-1 single-chain variable antibody fragment (scFv) was expressed at a high level as inclusion bodies in Escherichia coli. We refolded the scFv (Ka=2.35×10−7 M) by ion-exchange chromatography, dialysis, and dilution. The results showed that column chromatography refolding by high-performance Q Sepharose had remarkable advantages over conventional dilution and dialysis methods. Furthermore, the anti-ICAM-1 scFv yield of about 60 mg/L was higher with this method. The purity of the final product was greater than 90%, as shown by denaturing gel electrophoresis. Enzyme-linked immunosorbent assay, cell culture, and animal experiments were used to assess the immunological properties and biological activities of the renatured scFv.
| Reference Key |
sun2014brazilianexpression,
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| Authors | ;H. Sun;G.M. Wu;Y.Y. Chen;Y. Tian;Y.H. Yue;G.L. Zhang |
| Journal | Free radical biology & medicine |
| Year | 2014 |
| DOI |
10.1590/1414-431X20143276
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