ArticleScience signaling2020
The Myc tag monoclonal antibody 9E10 displays highly variable epitope recognition dependent on neighboring sequence context.
Article in Science signaling, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 28 citations in OpenAlex.
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- Bacterial surface display of human lectins in Escherichia coli.Microbial biotechnology · 2024Article
- A critical evaluation of protein kinase regulation by activation loop autophosphorylation.eLife · 2023Article
- Specific, sensitive and quantitative protein detection by in-gel fluorescence.Nature communications · 2023Article
- Breasi-CRISPR: an efficient genome-editing method to interrogate protein localization and protein-protein interactions in the embryonic mouse cortex.Development (Cambridge, England) · 2022Article
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- Identification of amino acid domains ofFrontiers in cellular and infection microbiology · 2022Article
- Fast-dissociating but highly specific antibodies are novel tools in biology, especially useful for multiplex super-resolution microscopy.STAR protocols · 2021Article
- A versatile nanoluciferase toolkit and optimized in-gel detection method for protein analysis in plants.Molecular breeding : new strategies in plant improvement · 2021Article
- A Novel KRAS Antibody Highlights a Regulation Mechanism of Post-Translational Modifications of KRAS during Tumorigenesis.International journal of molecular sciences · 2020Article
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- Fragile epitopes-Antibody's guess is as good as yours.Science signaling · 2020Article
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4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Epitope tags are short, linear antibody recognition sequences that enable detection of tagged fusion proteins by antibodies. Epitope tag position and neighboring sequences potentially affect its recognition by antibodies, and such context-dependent differences in tag binding may have a wide-ranging effect on data interpretation. We tested by Western blotting six antibodies that recognize the c-Myc epitope tag, including monoclonal antibodies 9E10, 4A6, 9B11, and 71D10 and polyclonal antibodies 9106 and A-14. All displayed context-dependent differences in their ability to detect N- or C-terminal Myc-tagged proteins. In particular, clone 9E10, the most cited Myc-tag antibody, displayed high context-dependent detection variability, whereas others, notably 4A6 and 9B11, showed much less context sensitivity in their detection of Myc-tagged proteins. The very high context sensitivity of 9E10 was further substantiated by peptide microarray analyses. We conclude that recently developed, purpose-made monoclonal antibodies specific for Myc have much more uniform reactivity in diverse assays and are much less context sensitive than is the legacy antibody 9E10.
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