ArticleBrazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica2014
Expression, production, and renaturation of a functional single-chain variable antibody fragment (scFv) against human ICAM-1.
Article in Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Recombinant single-chain variable fragment-based immunoassay for the authentication of Vietnamese ginseng via quantitative detection of majonoside R2.Journal of ginseng research · 2026Article
- Recovering ImmunogenicVaccines · 2025Article
- Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024Review
- Dopamine DBiomolecules · 2022Article
- Article
- Development of alkaline phosphatase-scFv and its use for one-step enzyme-linked immunosorbent assay for His-tagged protein detection.Open life sciences · 2022Article
- Anti-CXCR4 Single-Chain Variable Fragment Antibodies Have Anti-Tumor Activity.Frontiers in oncology · 2020Article
- Evaluation of scFv protein recovery from E. coli by in vitro refolding and mild solubilization process.Microbial cell factories · 2019Article
- The production of a recombinant tandem single chain fragment variable capable of binding prolamins triggering celiac disease.BMC biotechnology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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