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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The 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 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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 601–640 of 640
Monoclonal antibody generation by phage display: history, state-of-the-art, and future
Hentrich, C., Ylera, F., Frisch, C., & Knappik, A. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-95509-6.00001-x
B Cell and Autoimmune Diseases
Gao, J., Xu, Y., Li, Y., Yang, H., & Liu, W. (2025) · Springer eBooks · doi:10.1007/978-981-96-1027-3_8
The case for calibration-free concentration analysis
Chilewski, S. D. (2025) · Bioanalysis · doi:10.1080/17576180.2025.2517530
Matsubara, D. K., Park, P., Cuccovia, I. M., & Chaimovich, H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.06.680738
Heine, P. A., Nosenko, T., Kistner, S., Oliphant, K. D., Hanke‐Uhe, M., Shahid, A., Hu, B., Kucklick, M., Lehmler, N., Becker, M., et al. (2025) · Plant Biotechnology Journal · doi:10.1111/pbi.70431
Long-term Storage of Diluted Antibody in Tris-buffered Saline with Tween 20
Kwon, S., Park, H., Song, M., Cho, E., Lee, J. H., Kim, M. R., Seo, Y. W., Lim, Y. K., Lee, S. Y., & Kim, G. (2025) · Biological Procedures Online · doi:10.1186/s12575-025-00313-1
Application of a 2A-peptide system for polycistronic human IgG production in Leishmania tarentolae
Lai, J. Y., Tan, N. H., Tan, C. H., Choong, Y. S., & Lim, T. S. (2025) · Methods · doi:10.1016/j.ymeth.2025.12.005
Additional file 1 of A recombinant antibody toolbox for Dictyostelium discoideum
de Lima, W. C., Hammel, P., & Cosson, P. (2020) · Figshare · doi:10.6084/m9.figshare.12114717
Sourcing and screening human antibody repertoires for discovering biotherapeutics
Abdiche, Y. N., & Hoet, R. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00062-5
Garelja, M. L., Rees, T. A., & Hay, D. L. (2026) · Headache The Journal of Head and Face Pain · doi:10.1111/head.70020
Weiner, M. P. (2025) · BioTechniques · doi:10.1080/07366205.2026.2619165
Fonseca, M. F., Becker-Finco, A., Prado-Costa, B., Coelho, G. R., Weber-Lima, M. M., Muzzi, J. C. D., Jiacomini, I. G., Beltramino, M., Freitas-de-Sousa, L. A., Clissa, P. B., et al. (2026) · Toxicon · doi:10.1016/j.toxicon.2026.109022
Designed peptides as affinity ligands for extracellular-vesicle-based cancer diagnosis
Sarma, S., Park, J., Cho, Y. K., Tapdiya, A., Woo, H.-K., Lee, H., & Hall, C. K. (2026) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2026.118584
When RNA goes off script: ensuring transcript fidelity in transgene expression
Anderson, R., Ausler, C., & Jain, A. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00733-z
Dias, C., Villa, C., Carriço-Sá, B., Costa, R. C. B., Mafra, I., Pereira, C. M. D. M., & Costa, J. S. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.108807
Identification of antibodies by phage display for immunohistochemical applications
Mairaville, C. (2021) · theses.fr (ABES) · doi:10.70675/bbe469baz5631z452fzac83z2f6eaab87007
Tertel, T., Bauer, F. N., Stambouli, O., Kasimir‐Bauer, S., Keup, C., Lang, S., Sak, A., Stuschke, M., Rassaf, T., Schuler, M., et al. (2026) · Journal of Extracellular Biology · doi:10.1002/jex2.70144
Engineered protein nanoclusters reduce liver fibrosis and hepatocellular carcinoma in mice models
Saxena, T., Guedes, G., Domingues, I., Yagoubi, H., Guilbaud, L., den Bossche, W. V., Pangua, C., Velde, G. V., Učakar, B., Garcia‐Esnaola, A., et al. (2026) · Bioactive Materials · doi:10.1016/j.bioactmat.2026.05.038
Fernandes, G., Wang, W., Parwani, A. V., Ahmadian, S. S., Alves, M. J., Philips, J. J., & Otero, J. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.04.730099
Gere-Becker, M., Funk, L.-M., Groeger, M., Kilisch, M., Najafi, P., Koenig, F., Aloisi, F., Song, X., Davis, L. C., Galione, A., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.30.735531
Ultrastructural approaches to localize and quantify plasma membrane proteins in neurons
Aguado, C., Alfaro‐Ruiz, R., Martínez-Poyato, M. L., & Luján, R. (2026) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2026.07.029
Functional Parameters of Hybridoma Cells: Methods of Evaluation and Biotechnological Relevance
Bezukladnikova, T., Анатольевна, З. С., Lazarev, S. S., & Rayev, M. B. B. (2026) · Antibodies · doi:10.3390/antib15040067
Zhang, Y., Long-xin, Y., Cai, Z.-X., Yin, M.-Z., Song, L., Li, J.-H., Zhang, H., Li, H.-Y., Shi, H., & Wang, X.-H. (2026) · Microchimica Acta · doi:10.1007/s00604-026-08336-5
Commentary – Non-animal-derived antibodies: addressing ethical and scientific needs
Bailey, J., & McCarthy, J. (2026) · Antibody Reports · doi:10.24450/journals/abrep.2026.e2553
Evaluating novel antibodies for cytokine profiling in the guinea pig model
Maristela, L., Longworth, A., Ackart, D. F., Lanni, F., Gibb, J., Freedman, A., Miller, O. R., Cai, L., Qi, H., Baldwin, S. L., et al. (2026) · ImmunoHorizons · doi:10.1093/immhor/vlag051
Reproducibility in biomedical research
Zhong, J., D’Angelo, D., Lyu, C., Xu, I., Enns, P. K., Wang, F., & Kaushal, R. (2026) · Nature Medicine · doi:10.1038/s41591-026-04667-1
Xu, Q., Le, T., Luo, Z., Ly, C. P., Yan, Y., & Zheng, Y. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.25.754510
Better antibodies, better science
Duchêne, J. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3004001
Wang, H., Wang, R., Cai, G., & Jia, Q. (2026) · Analytical Methods · doi:10.1039/d6ay01390b
Higashiizumi, E., Shimizu, H., Nishikawa, T., Koyama, K., Nakagawa, H., Nakatani, N., Tachibana, T., Murray, M. E., Dickson, D. W., Kakita, A., et al. (2026) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlag103
FAIRsharing record for: ABCD database
FAIRsharing Team (2018) · FAIRsharing.org · doi:10.25504/fairsharing.z8oki5
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
