ArticleScientific reports2016
A detergent-based procedure for the preparation of IgG-like bispecific antibodies in high yield.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Exploring Synergistic Potential of Sorafenib and Atorvastatin to Launch Apoptosis and Ferroptosis-driven Mixed Cell Death Mechanism in Colorectal Cancer.AAPS PharmSciTech · 2026Article
- SureCLIP and DrCLIP: Genetic manipulation-free, generalizable interactome mapping for cells and zebrafish.bioRxiv : the preprint server for biology · 2025Article
- Topical vaginal drug therapy in cervical cancer management: a review of clinical trials and preclinical evidence.Medical oncology (Northwood, London, England) · 2025Review
- B cells secrete functional antigen-specific IgG antibodies on extracellular vesicles.Scientific reports · 2024Article
- First site-specific conjugation method for native goat IgG antibodies via glycan remodeling at the conserved Fc region.Antibody therapeutics · 2024Article
- Article
- Multiplex Staining by Sequential Immunostaining and Antibody Removal on Routine Tissue Sections.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2017Article
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Authors and funding
5 authors.
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Abstract
Bispecific antibodies (BsAbs), with the ability to recognize two different epitopes simultaneously, offer remarkable advantages in bioassays, cancer therapy, biosensors, and enzyme electrodes. Preparation and purification of BsAbs in adequate quantities remains a major hurdle in their use in various applications. Poor yield is also the principal limitation in the preparation of BsAbs by the redox procedure. IgG with reduced inter-heavy chain disulfides do not dissociate into half molecules at neutral pH. In this study, we report that the dissociation occurs in presence of sodium dodecyl sulphate (SDS) and inclusion of the detergent during the redox procedure results in remarkable increase in the formation of the BsAbs. Exposure of antibodies to 0.1% (w/v) SDS causes only minor loss in secondary/tertiary structure and the ability to bind the antigen. The BsAbs prepared using the modified redox procedure that recognize the antigens HRP and α-LA were prepared and successfully employed for detecting α-LA in milk/dairy products by ELISA and dot blot techniques. BsAbs were also prepared from partially purified immunoglobulin gamma (IgG). This work shows for the first time that SDS, by dissociating IgG with reduced inter-heavy chain disulfides into half molecules, markedly enhances the formation of BsAbs by the redox procedure.
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