ArticleJournal of industrial microbiology & biotechnology2014
Functional expression of a single-chain antibody fragment against human epidermal growth factor receptor 2 (HER2) in Escherichia coli.
Article in Journal of industrial microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Expression and functional characterization of an anti-CD22 scFv targeting B-cell malignancies.Research in pharmaceutical sciences · 2025Article
- Evaluation of the Safety of A Novel Anti-HER2 Immunotoxin Containing Modified Fragment ofIranian journal of biotechnology · 2025Article
- Integrated bioprocessing and genetic strategies to enhance soluble expression of anti-HER2 immunotoxin in E. Coli.AMB Express · 2024Article
- Design and construction of scFv-PE35KDEL as a novel immunotoxin against human epidermal growth factor receptor 2 for cancer therapy.Biotechnology letters · 2023Article
- Therapeutic potential of a novel IP-10-(anti-HER2 scFv) fusion protein for the treatment of HER2-positive breast cancer.Biotechnology letters · 2023Article
- Different strategies for expression and purification of the CT26-poly-neoepitopes vaccine in Escherichia coli.Molecular biology reports · 2022Article
- Co-Expression of Chaperones for Improvement of Soluble Expression and Purification of An Anti-HER2 scFv inAdvanced biomedical research · 2022Article
- Effects of variable domain orientation on anti-HER2 single-chain variable fragment antibody expressed in the Escherichia coli cytoplasm.Biotechnology progress · 2021Article
- Evolution ofInternational journal of molecular sciences · 2020Review
- Evaluation of soluble expression of recombinant granulocyte macrophage stimulating factor (rGM-CSF) by three differentResearch in pharmaceutical sciences · 2020Article
- Optimization of Buffer Additives for Efficient Recovery of hGM-CSF from Inclusion Bodies Using Response Surface Methodology.Iranian journal of pharmaceutical research : IJPR · 2020Article
- Anti-HER2 scFv Expression in Escherichia coli SHuffleMolecular biotechnology · 2020Article
- The HER2 S310F Mutant Can Form an Active Heterodimer with the EGFR, Which Can Be Inhibited by Cetuximab but Not by Trastuzumab as well as Pertuzumab.Biomolecules · 2019Article
- Improvement of solubility and refolding of an anti-human epidermal growth factor receptor 2 single-chain antibody fragment inclusion bodies.Research in pharmaceutical sciences · 2018Article
- A single-domain antibody-linked Fab bispecific antibody Her2-S-Fab has potent cytotoxicity against Her2-expressing tumor cells.AMB Express · 2016Article
- Expression of V(H)-linker-V(L) orientation-dependent single-chain Fv antibody fragment derived from hybridoma 2E6 against aflatoxin B1 in Escherichia coli.Journal of industrial microbiology & biotechnology · 2015Article
- Optimization of a single-chain antibody fragment overexpression in Escherichia coli using response surface methodology.Research in pharmaceutical sciencesArticle
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human epidermal growth factor receptor (HER) family plays an important role in cell growth and signaling and alteration of its function has been demonstrated in many different kinds of cancer. Receptor dimerization is necessary for the HER signal transduction pathway and tyrosine kinase activity. Recently, several monoclonal antibodies have been developed to directly interfere with ligand-HER receptor binding and receptor dimerization. A single chain variable fragment (ScFv) is a valuable alternative to an intact antibody. This report describes the production and purification of an ScFv specific for domain II of the HER2 receptor in Escherichia coli BL21 (DE3) cytoplasm. The majority of expressed of anti-her2his-ScFv protein was produced as inclusion bodies. A Ni-NTA affinity column was used to purify the anti-her2his-ScFv protein. The molecular weight of anti-her2his-ScFv protein was estimated to be approximately 27 kDa, as confirmed by SDS-PAGE and Western blotting assay. The anti-her2his-ScFv showed near 95 % purity and reached a yield of approximately 29 mg/l in flask fermentation. The purified anti-her2his-ScFv showed its biological activity by binding to HER2 receptor on the surface of BT-474 cells. This ScFv may be a potential pharmaceutical candidate for targeting tumour cells overexpressing HER2 receptor.
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