The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Reproducibility: Standardize antibodies used in research
Open accessAbstract
To save millions of dollars and dramatically improve reproducibility, protein-binding reagents must be defined by their sequences and produced as recombinant proteins, say Andrew Bradbury, Andreas Plückthun and 110 co-signatories.
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“This observation has been followed by a number of additional reports, the summary of which is, in essence, that 77-90% of biomedical experiments are not reproducible [14-17].”
From Guidelines for the use of flow cytometry and cell sorting in immunological studies (third edition) (2021) · cites this paper as [14]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Sequence-defined or recombinant products can improve traceability and manufacturing consistency relative to reagents purified directly from animal tissues or biological fluids, which are often chemically undefined (Bradbury and Plückthun, 2015).”
From Challenges and solutions in transitioning to animal-free standards: a comprehensive analysis of components in human cell-based developmental neurotoxicity assays (2026) · cites this paper as Bradbury and Plückthun, 2015
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“This hybridoma-to-recombinant progression in NPC2-5 assays mirrors broader trends toward animal-free antibody production that eliminates batch variability while enabling molecular engineering opportunities such as affinity maturation and multi-formatting (humanization, Fc-modifications) (Bradbury and Plückthun, 2015; Bradbury et al., 2021).”
From Challenges and solutions in transitioning to animal-free standards: a comprehensive analysis of components in human cell-based developmental neurotoxicity assays (2026) · cites this paper as Bradbury and Plückthun, 2015
Experimental — accuracy not yet measuredIn the citing paper
“However, antibodies possess many inherent limitations: batch-to-batch variation, high cost of production, poor chemical stability, and lack of proteoform-specific epitope recognition that collectively contribute to reproducibility issues [62–64].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [64]
In the citing paper
“However, antibody-based platforms suffer from significant limitations including the batch-to-batch variability, high cost of the antibody production, and relatively low chemical stability14,15.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [15]
In the citing paper
“Thus, these NPs can serve as replacements to conventional immuno-based techniques to overcome the antibody-related limitations in cTnI immunoassays and potentially address the current reproducibility crisis caused by antibodies in general14–16,51,53.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [15]
In the citing paper
“These serum cTnI enrichment results illustrate the major benefits of functionalized NPs compared to current antibody-based approaches: (1) NPs are capable of reproducibly and effectively enriching cTnI (Supplementary Fig. 23) across all tested serum samples without the use of antibody, thus overcoming the intrinsic antibody-related limitations (vide supra)14,15,51–53.”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [15]
In the citing paper
“These results highlight the unique advantages that these functionalized NPs possess for protein enrichment over antibody-based platforms: (a) comparable size and diffusion kinetics to proteins, promoting effective capture of low-abundance proteins within complex mixtures20,47,48; (b) high surface area per volume and high number of flexible binding sites, contributing to high ligand density and”
From Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum (2020) · cites this paper as [15]
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Citations
Cites
Continuous cultures of fused cells secreting antibody of predefined specificity
Köhler, G., & Milstein, C. (1975) · Nature · doi:10.1038/256495a0 · Cited by 17,200
Raise standards for preclinical cancer research
Begley, C. G., & Ellis, L. M. (2012) · Nature · doi:10.1038/483531a · Cited by 2,979
Policy: NIH plans to enhance reproducibility
Collins, F. S., & Tabak, L. A. (2014) · Nature · doi:10.1038/505612a · Cited by 1,247
Engineering novel binding proteins from nonimmunoglobulin domains
Binz, H. K., Amstutz, P., & Plückthun, A. (2005) · Nature Biotechnology · doi:10.1038/nbt1127 · Cited by 676
Self-citationA Genecentric Human Protein Atlas for Expression Profiles Based on Antibodies
Berglund, L., Björling, E., Oksvold, P., Fagerberg, L., Asplund, A., Szigyarto, C. A., Persson, A. B., Ottosson, J. E. A., Wernérus, H., Nilsson, P., et al. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r800013-mcp200 · Cited by 671
Bordeaux, J., Welsh, A. W., Agarwal, S., Killiam, E. J., Baquero, M. T., Hanna, J. A., Anagnostou, V., & Rimm, D. L. (2010) · BioTechniques · doi:10.2144/000113382 · Cited by 597
Vasilevsky, N. A., Brush, M. H., Paddock, H., Ponting, L., Tripathy, S. J., LaRocca, G. M., & Haendel, M. A. (2013) · PeerJ · doi:10.7717/peerj.148 · Cited by 271
Aptamers and the RNA World, Past and PresentPreprint
Gold, L., Janjić, N., Jarvis, T. C., Schneider, D., Walker, J. J., Wilcox, S. K., & Zichi, D. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003582 · Cited by 119
Commercial antibodies and their validation
Voskuil, J. L. A. (2014) · F1000Research · doi:10.12688/f1000research.4966.2 · Cited by 82
Commercial antibodies and their validation
Voskuil, J. (2014) · F1000Research · doi:10.12688/f1000research.4966.1 · Cited by 82
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Fluorescence nanoscopy in cell biology
Sahl, S. J., Hell, S. W., & Jakobs, S. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.71 · Cited by 996
Analysis of aptamer discovery and technology
Dunn, M. R., Jimenez, R. M., & Chaput, J. C. (2017) · Nature Reviews Chemistry · doi:10.1038/s41570-017-0076 · Cited by 938
Reproducibility crisis: Blame it on the antibodies
Baker, M. (2015) · Nature · doi:10.1038/521274a · Cited by 830
A proposal for validation of antibodies
Uhlen, M., Bandrowski, A., Carr, S., Edwards, A., Ellenberg, J., Lundberg, E., Rimm, D. L., Rodriguez, H., Hiltke, T., Snyder, M., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3995 · Cited by 626
Protein Phosphorylation: A Major Switch Mechanism for Metabolic Regulation
Humphrey, S. J., James, D. E., & Mann, M. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.013 · Cited by 574
Metadata
- Authors
- Bradbury, A., & Plückthun, A.
- Affiliations
- Los Alamos National Laboratory (US)
- University of Zurich (CH)
- Corresponding author
- Bradbury, Andrew
- Venue
- Nature
- Published
- 2015-02-04
- Volume
- 518
- Issue
- 7537
- Pages
- 27-29
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2122225224
- Cited by
- 647
- References
- 10
- Citations by year
- 2026: 34 · 2025: 44 · 2024: 36 · 2023: 46 · 2022: 56 · 2021: 49 · 2020: 68 · 2019: 51 · 2018: 69 · 2017: 61 · 2016: 65 · 2015: 66
- FWCI
- 70.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature (publishedVersion, public-domain)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
- Zurich Open Repository and Archive (University of Zurich)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Health Sciences › Veterinary › Small Animals › Animal testing and alternatives
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Advanced Biosensing Techniques and Applications
- Keywords
- antibody standardization, recombinant antibodies, research reproducibility, antibody production
- MeSH terms
- Amino Acid Sequence, Antibodies, Antibodies, Monoclonal, Antibody Specificity, Hybridomas, Immune Sera, Indicators and Reagents, Quality Control, Recombinant Proteins, Reproducibility of Results, Biomedical Research
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