ArticleBiotechnology progress2018
Development of a novel affinity chromatography resin for platform purification of bispecific antibodies with modified protein a binding avidity.
Article in Biotechnology progress, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- The Production and Purification of Therapeutic Antibodies: A Comprehensive Analysis of Process- and Product-Related Contaminants.Biomolecules · 2026Review
- Molecule Formats of B-Cell Targeting Biologics: Applications in Autoimmune Disease Treatment and Impacts on Manufacturability.Pharmaceutics · 2025Review
- Advantages of MabSelect VH3, a novel VH3-specific Protein A resin, over its two conventional counterparts in purifying a VHH-based trispecific antibody.Journal of biological methods · 2025Article
- Next generation of multispecific antibody engineering.Antibody therapeutics · 2024Review
- Effective flow-through polishing strategies for knob-into-hole bispecific antibodies.Bioresources and bioprocessing · 2022Article
- The use of predictive models to develop chromatography-based purification processes.Frontiers in bioengineering and biotechnology · 2022Review
- Current trends and challenges in the downstream purification of bispecific antibodies.Antibody therapeutics · 2021Review
- Expanding the Boundaries of Biotherapeutics with Bispecific Antibodies.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2018Review
- Tuning Relative Polypeptide Expression to Optimize Assembly, Yield and Downstream Processing of Bispecific Antibodies.Antibodies (Basel, Switzerland) · 2018Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There is strong interest in the production of bispecific monoclonal antibodies that can simultaneously bind two distinct targets or epitopes to achieve novel mechanisms of action and efficacy. Regeneron's bispecific technology, based upon a standard IgG, consists of a heterodimer of two different heavy chains, and a common light chain. Coexpression of two heavy chains leads to the formation of two parental IgG impurities, the removal of which is facilitated by a dipeptide substitution in the Fc portion of one of the heavy chains that ablates Fc Protein A binding. Therefore, the affinity capture (Protein A) step of the purification process must perform both bulk capture and high resolution of these mAb impurities, a task current commercially available resins are not designed for. Resolution can be further impaired by the ability of Protein A to bind some antibodies in the variable region of the heavy chain (V
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Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.