ArticleBiochemistry and biophysics reports2018
Domain unfolding of monoclonal antibody fragments revealed by non-reducing SDS-PAGE.
Article in Biochemistry and biophysics reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Development and preliminary physicochemical characterization of a Ramucirumab biosimilar candidate in CHO cells using shake-flask fed-batch culture.Bioprocess and biosystems engineering · 2026Article
- Reformulation and Thermal Stability of a Therapeutic Anti-Cocaine mAb.Journal of pharmaceutical sciences · 2023Article
- Principles of deep immunohistochemistry for 3D histology.Cell reports methods · 2023Review
- Article
- Design and optimization of membrane chromatography for monoclonal antibody charge variant separation.Biotechnology progress · 2022Article
- Comparative analysis of plant transient expression vectors for targeted N-glycosylation.Frontiers in bioengineering and biotechnology · 2022Article
- Multi-domain unfolding of the Fab fragment of a humanized anti-cocaine mAb characterized by non-reducing SDS-PAGE.Biochemical and biophysical research communications · 2020Article
- Ligand binding to a humanized anti-cocaine mAb detected by non-reducing SDS-PAGE.Biochemistry and biophysics reports · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Monoclonal antibodies and derived fragments are used extensively both experimentally and therapeutically. Thorough characterization of such antibodies is necessary and includes assessment of their thermal and storage stabilities. Thus, assessment of the underlying conformational stabilities of the antibodies is also important. We recently documented that non-reducing SDS-PAGE can be used to assess both monoclonal and polyclonal IgG domain thermal unfolding in SDS. Utilizing this same h2E2 anti-cocaine mAb, in this study we generated and analyzed various mAb antibody fragments to delineate the structural domains of the antibody responsible for the observed discrete bands following various heating protocols and analysis by non-reducing SDS-PAGE. Previously, these domain unfolding transitions and gel bands were hypothesized to stem from known mAb structural domains based on the relative thermal stability of those CH2, CH3, and Fab domains in the absence of SDS, as measured by differential scanning calorimetry. In this study, we generated and analyzed F(ab')
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