ArticleAdvanced biomedical research2022
Co-Expression of Chaperones for Improvement of Soluble Expression and Purification of An Anti-HER2 scFv in
Article in Advanced biomedical research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Enhancing soluble expression and purification of a bispecific scFv antibody inResearch in pharmaceutical sciences · 2026Article
- Advancing the frontier of plant-based therapeutics: critical innovations in molecular farming and bioprocess Integration.Biotechnology letters · 2026Review
- Other Techniques.Advances in biochemical engineering/biotechnology · 2026Review
- Biopharming of Lactoferrin: Current Strategies and Future Prospects.Pharmaceutics · 2025Review
- Molecular chaperone effects on recombinant yield and binding characteristics of an ABA-specific scFv inFrontiers in bioengineering and biotechnology · 2025Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Single-chain fragment variable (scFv) is one of the most commonly used antibody fragments. They offer some advantages over full-length antibodies, including better penetration to target tissues. However, their functional production has been a challenge for manufacturers due to the potential misfolding and formation of inclusion bodies. Here we evaluated the soluble expression and purification of molecular chaperone co-expression. Materials and Methods: Results: SDS-PAGE analysis confirmed the successful co-expression of anti-HER2-scFv and DnaK/DnaJ/GrpE chaperones. Co-expression with chaperones and low-temperature cultivation synergistically improved the soluble expression of anti-HER2 scFv. Co-expression with chaperone also exhibited an approximately four-fold increase in the final yield of purified soluble protein. Conclusion: The combination of co-expression with chaperones and low temperature presented in this work may be useful for the improvement of commercial production of other scFvs in
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Registered trials
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