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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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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
Replacing antibodies with aptamers in lateral flow immunoassay
Chen, A., & Yang, S. (2015) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2015.04.041 · Cited by 560
Guidelines for the use of flow cytometry and cell sorting in immunological studies (third edition)
Cossarizza, A., Chang, H., Radbruch, A., Abrignani, S., Addo, R., Akdis, M., Andrä, I., Andreata, F., Annunziato, F., Arranz, E., et al. (2021) · European Journal of Immunology · doi:10.1002/eji.202170126 · Cited by 531
Stein, C. (2015) · Annual Review of Medicine · doi:10.1146/annurev-med-062613-093100 · Cited by 493
Precision diagnostics: moving towards protein biomarker signatures of clinical utility in cancer
Borrebaeck, C. A. K. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2016.153 · Cited by 441
Smith, J. C., Sausville, E. L., Girish, V., Yuan, M. L., Vasudevan, A., John, K. M., & Sheltzer, J. M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.05.012 · Cited by 431
The 2015 super-resolution microscopy roadmap
Hell, S. W., Sahl, S. J., Bates, M., Zhuang, X., Heintzmann, R., Booth, M. J., Bewersdorf, J., Shtengel, G. E., Hess, H. F., Tinnefeld, P., et al. (2015) · Journal of Physics D Applied Physics · doi:10.1088/0022-3727/48/44/443001 · Cited by 355
Switchable Fluorophores for Single-Molecule Localization Microscopy
Li, H., & Vaughan, J. C. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00767 · Cited by 319
Protein purification and analysis: next generation Western blotting techniques
Mishra, M., Tiwari, S., & Gomes, A. V. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2017.1388167 · Cited by 305
De novo design of high-affinity binders of bioactive helical peptides
Torres, S. V., Leung, P. J. Y., Venkatesh, P., Lutz, I. D., Hink, F., Huynh, H., Becker, J. O., Yeh, A. H.-W., Juergens, D., Bennett, N. R., et al. (2023) · Nature · doi:10.1038/s41586-023-06953-1 · Cited by 287
Insufficient antibody validation challenges oestrogen receptor beta research
Andersson, S., Sundberg, M., Pristovšek, N., Ibrahim, A. A., Jonsson, P., Katona, B., Clausson, C.-M., Zieba, A., Ramström, M., Söderberg, O., et al. (2017) · Nature Communications · doi:10.1038/ncomms15840 · Cited by 249
Soh, J. H., Chan, H., & Ying, J. Y. (2020) · Nano Today · doi:10.1016/j.nantod.2019.100831 · Cited by 236
Multiplexed Epitope-Based Tissue Imaging for Discovery and Healthcare Applications
Bodenmiller, B. (2016) · Cell Systems · doi:10.1016/j.cels.2016.03.008 · Cited by 235
Nanobodies and recombinant binders in cell biology
Helma, J., Cardoso, M. C., Muyldermans, S., & Leonhardt, H. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201409074 · Cited by 228
Affimer proteins are versatile and renewable affinity reagents
Tiede, C., Bedford, R., Heseltine, S. J., Smith, G. A., Wijetunga, I., Ross, R. L., AlQallaf, D., Roberts, A. P. E., Balls, A., Curd, A., et al. (2017) · eLife · doi:10.7554/elife.24903 · Cited by 206
Western Blotting (immunoblotting): History, Theory, Uses, Protocol and Problems
Sule, R. O., Rivera, G. D. T., & Gomes, A. V. (2023) · BioTechniques · doi:10.2144/btn-2022-0034 · Cited by 192
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Melby, J. A., Roberts, D. S., Larson, E. J., Brown, K. A., Bayne, E. F., Jin, S., & Ge, Y. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00099 · Cited by 201
Advancements in Aptamer Discovery Technologies
Gotrik, M. R., Feagin, T., Csordas, A. T., Nakamoto, M. A., & Soh, H. T. (2016) · Accounts of Chemical Research · doi:10.1021/acs.accounts.6b00283 · Cited by 176
Single-Domain Antibodies As Versatile Affinity Reagents for Analytical and Diagnostic Applications
González‐Sapienza, G., Rossotti, M. A., & Rosa, S. T.-D. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00977 · Cited by 181
New concepts in opioid analgesia
Stein, C. (2018) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2018.1516204 · Cited by 175
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Valihrach, L., Androvic, P., & Kubista, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030807 · Cited by 168
Unpicking the proteome in single cells
Slavov, N. (2020) · Science · doi:10.1126/science.aaz6695 · Cited by 165
Active promoters give rise to false positive ‘Phantom Peaks’ in ChIP-seq experiments
Jain, D., Baldi, S., Zabel, A., Straub, T., & Becker, P. B. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv637 · Cited by 156
Laflamme, C., McKeever, P. M., Kumar, R., Schwartz, J., Kolahdouzan, M., Chen, C. X., You, Z., Benaliouad, F., Gileadi, O., McBride, H. M., et al. (2019) · eLife · doi:10.7554/elife.48363 · Cited by 155
Top-down proteomics: challenges, innovations, and applications in basic and clinical research
Brown, K. A., Melby, J. A., Roberts, D. S., & Ge, Y. (2020) · Expert Review of Proteomics · doi:10.1080/14789450.2020.1855982 · Cited by 152
Roberts, D. S., Loo, J. A., Tsybin, Y. O., Liu, X., Wu, S., Chamot-Rooke, J., Agar, J. N., Paša-Tolić, L., Smith, L. M., & Ge, Y. (2024) · Nature Reviews Methods Primers · doi:10.1038/s43586-024-00318-2 · Cited by 161
Three-dimensional map of nonhematopoietic bone and bone-marrow cells and molecules
Coutu, D. L., Kokkaliaris, K. D., Kunz, L., & Schroeder, T. (2017) · Nature Biotechnology · doi:10.1038/nbt.4006 · Cited by 151
A toolbox of anti–mouse and anti–rabbit IgG secondary nanobodies
Pleiner, T., Bates, M., & Görlich, D. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201709115 · Cited by 155
Mohammadinejad, R., Shavandi, A., Raie, D. S., Sangeetha, J., Soleimani, M., Hajibehzad, S. S., Thangadurai, D., Hospet, R., Popoola, J. O., Arzani, A., et al. (2019) · Green Chemistry · doi:10.1039/c9gc00335e · Cited by 147
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Ascoli, C. A., & Aggeler, B. (2018) · BioTechniques · doi:10.2144/btn-2018-0065 · Cited by 142
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Laustsen, A. H., Greiff, V., Karatt-Vellatt, A., Muyldermans, S., & Jenkins, T. P. (2021) · Trends in Biotechnology · doi:10.1016/j.tibtech.2021.03.003 · Cited by 147
Antibody anarchy: A call to order
Baker, M. (2015) · Nature · doi:10.1038/527545a · Cited by 140
Modern affinity reagents: Recombinant antibodies and aptamers
Groff, K., Brown, J., & Clippinger, A. J. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.10.004 · Cited by 146
Mass spectrometry–based protein identification in proteomics—a review
Noor, Z., Ahn, S. B., Baker, M. S., Ranganathan, S., & Mohamedali, A. (2019) · Briefings in Bioinformatics · doi:10.1093/bib/bbz163 · Cited by 147
Principles for computational design of binding antibodies
Baran, D., Pszolla, M. G., Lapidoth, G. D., Norn, C., Dym, O., Unger, T., Albeck, S., Tyka, M. D., & Fleishman, S. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707171114 · Cited by 136
Third generation antibody discovery methods: in silico rational design
Sormanni, P., Aprile, F. A., & Vendruscolo, M. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00523k · Cited by 143
Parisi, O. I., Francomano, F., Dattilo, M., Patitucci, F., Prete, S., Amone, F., & Puoci, F. (2022) · Journal of Functional Biomaterials · doi:10.3390/jfb13010012 · Cited by 142
Chang, Y.-F., Wang, W., Hong, Y.-W., Yuan, R.-Y., Chen, K.-H., Huang, Y.-W., Lu, P., Chen, Y., Chen, Y. A., Su, L., et al. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b03934 · Cited by 130
Marcon, E., Jain, H., Bhattacharya, A., Guo, H., Phanse, S., Pu, S., Byram, G., Collins, B. C., Dowdell, E., Fenner, M., et al. (2015) · Nature Methods · doi:10.1038/nmeth.3472 · Cited by 128
Generating Biologically Stable TNA Aptamers that Function with High Affinity and Thermal Stability
Dunn, M. R., McCloskey, C. M., Buckley, P. E., Rhea, K. A., & Chaput, J. C. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c00641 · Cited by 120
Bauer, M., Strom, M., Hammond, D., & Shigdar, S. L. (2019) · Molecules · doi:10.3390/molecules24234377 · Cited by 119
Quality Issues of Research Antibodies
Weller, M. (2016) · Analytical Chemistry Insights · doi:10.4137/aci.s31614 · Cited by 110
Never waste a good crisis: confronting reproducibility in translational research
Drucker, D. J. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.006 · Cited by 117
Bradbury, A. R. M., Trinklein, N. D., Thie, H., Wilkinson, I. C., Tandon, A. K., Anderson, S., Bladen, C. L., Jones, B., Aldred, S. F., Bestagno, M., et al. (2018) · mAbs · doi:10.1080/19420862.2018.1445456 · Cited by 121
Self-citationA perception-based nanosensor platform to detect cancer biomarkers
Yaari, Z. A., Yang, Y., Apfelbaum, E., Cupo, C., Settle, A. H., Cullen, Q., Cai, W., Roche, K. L., Levine, D. A., Fleisher, M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abj0852 · Cited by 115
A comparative analysis of cell surface targeting aptamers
Kelly, L., Maier, K. E., Yan, A. C., & Levy, M. (2021) · Nature Communications · doi:10.1038/s41467-021-26463-w · Cited by 114
Tan, X., Constantin, T. P., Sloane, K. L., Waggoner, A. S., Bruchez, M. P., & Armitage, B. A. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b04211 · Cited by 114
Ayoubi, R., Ryan, J., Biddle, M., Alshafie, W., Fotouhi, M., Bolívar, S. G., Moleón, V. R., Eckmann, P., Worrall, D., McDowell, I., et al. (2023) · eLife · doi:10.7554/elife.91645 · Cited by 110
Transient expression of human antibodies in mammalian cells
Vazquez-Lombardi, R., Névoltris, D., Luthra, A., Schofield, P., Zimmermann, C., & Christ, D. (2017) · Nature Protocols · doi:10.1038/nprot.2017.126 · Cited by 113
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Uchański, T., Zögg, T., Yin, J., Yuan, D., Wohlkönig, A., Fischer, B., Rosenbaum, D. M., Kobilka, B. K., Pardon, E., & Steyaert, J. (2019) · Scientific Reports · doi:10.1038/s41598-018-37212-3 · Cited by 114
Animal-derived products in science and current alternatives
Duarte, A. C., Costa, E. C., Filipe, H. A. L., Saraiva, S. M., Jacinto, T., Miguel, S. P., Ribeiro, M. P., & Coutinho, P. (2023) · Biomaterials Advances · doi:10.1016/j.bioadv.2023.213428 · Cited by 117
COVID-19: A challenge for electrochemical biosensors
Kudr, J., Michálek, P., Ilieva, L., Adam, V., & Zítka, O. (2021) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2021.116192 · Cited by 112
Gilda, J. E., Ghosh, R., Cheah, J. X., West, T. M., Bodine, S. C., & Gomes, A. V. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135392 · Cited by 124
A High Through-put Platform for Recombinant Antibodies to Folded Proteins
Hornsby, M. J., Paduch, M., Miersch, S., Sääf, A. M., Matsuguchi, T., Lee, B. H., Wypisniak, K., Doak, A. K., King, D., Usatyuk, S., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.052209 · Cited by 106
Animal‐free alternatives and the antibody iceberg
Gray, A., Bradbury, A. R. M., Knappik, A., Plückthun, A., Borrebaeck, C. A. K., & Dübel, S. (2020) · Nature Biotechnology · doi:10.1038/s41587-020-0687-9 · Cited by 111
Self-citationA Scalable Genome-Editing-Based Approach for Mapping Multiprotein Complexes in Human Cells
Dalvai, M., Loehr, J., Jacquet, K., Huard, C., Lopez‐Roques, C., Herst, P. M., Côté, J., & Doyon, Y. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.009 · Cited by 113
Bai, X., Wang, L.-H., Ren, J., Bai, X.-W., Zeng, L., Shen, A., & Hu, J. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05153 · Cited by 106
Improving natural product research translation: From source to clinical trial
Sorkin, B. C., Kuszak, A. J., Bloss, G., Fukagawa, N. K., Hoffman, F. A., Jafari, M., Barrett, B. P., Brown, P. N., Bushman, F. D., Casper, S. J., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201902143r · Cited by 110
Analytical techniques for multiplex analysis of protein biomarkers
van Gool, A. J., Corrales, F. J., Čolović, M. B., Krstic, D. Z., Oliver‐Martos, B., Martínez-Cáceres, E. M., Jakaša, I., Gajski, G., Brun, V., Kyriacou, K. C., et al. (2020) · Expert Review of Proteomics · doi:10.1080/14789450.2020.1763174 · Cited by 109
Reproducibility2020: Progress and priorities
Freedman, L. P., Venugopalan, G., & Wisman, R. (2017) · F1000Research · doi:10.12688/f1000research.11334.1 · Cited by 102
Plug-and-Play Protein Modification Using Homology-Independent Universal Genome Engineering
Gao, Y., Hisey, E. E., Bradshaw, T. W., Erata, E., Brown, W. E., Courtland, J. L., Uezu, A., Xiang, Y., Diao, Y., & Soderling, S. H. (2019) · Neuron · doi:10.1016/j.neuron.2019.05.047 · Cited by 108
Enhanced validation of antibodies for research applications
Edfors, F., Hober, A., Linderbäck, K., Maddalo, G., Azimi, A., Sivertsson, Å., Tegel, H., Hober, S., Szigyarto, C. A., Fagerberg, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06642-y · Cited by 104
Multianalyte Antibiotic Detection on an Electrochemical Microfluidic Platform
Kling, A., Chatelle, C. V., Armbrecht, L., Qelibari, E., Kieninger, J., Dincer, C., Weber, W., & Urban, G. A. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02294 · Cited by 96
Recombinant antibodies and their use for food immunoanalysis
Peltomaa, R., Barderas, R., Benito‐Peña, E., & Moreno‐Bondi, M. C. (2021) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03619-7 · Cited by 95
Fifty years of monoclonals: the past, present and future of antibody therapeutics
Chan, A. C., Martyn, G. D., & Carter, P. J. (2025) · Nature reviews. Immunology · doi:10.1038/s41577-025-01207-9 · Cited by 104
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Cheikhi, A., Barchowsky, A., Sahu, A., Shinde, S. N., Pius, A., Clemens, Z. J., Li, H., Kennedy, C. A., Hoeck, J. D., Franti, M., et al. (2019) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glz061 · Cited by 92
Parola, C., Neumeier, D., & Reddy, S. T. (2017) · Immunology · doi:10.1111/imm.12838 · Cited by 94
Morphological single cell profiling of the epithelial–mesenchymal transition
Leggett, S. E., Sim, J. Y., Rubins, J. E., Neronha, Z. J., Williams, E. K., & Wong, I. Y. (2016) · Integrative Biology · doi:10.1039/c6ib00139d · Cited by 90
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Syu, G., Dunn, J., & Zhu, H. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r120.001936 · Cited by 90
Feature-rich covalent stains for super-resolution and cleared tissue fluorescence microscopy
Mao, C., Lee, M. Y., Jhan, J.-R., Halpern, A. R., Woodworth, M. A., Glaser, A. K., Chozinski, T. J., Shin, L., Pippin, J. W., Shankland, S. J., et al. (2020) · Science Advances · doi:10.1126/sciadv.aba4542 · Cited by 86
Chiron, C., Tompkins, T. A., & Burguière, P. (2017) · Journal of Applied Microbiology · doi:10.1111/jam.13666 · Cited by 85
Butler, T. A. J., Paúl, J., Chan, E., Smith, R., & Tolosa, J. M. (2019) · BioMed Research International · doi:10.1155/2019/5214821 · Cited by 91
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Signore, M., Manganelli, V., & Hodge, A. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6990-6_4 · Cited by 84
Filograna, R., Civiero, L., Ferrari, V., Codolo, G., Greggio, E., Bubacco, L., Beltramini, M., & Bisaglia, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136769 · Cited by 82
Generation of Murine Monoclonal Antibodies by Hybridoma Technology
Holzlöhner, P., & Hanack, K. (2017) · Journal of Visualized Experiments · doi:10.3791/54832 · Cited by 81
Li, J., Wang, J., Grewal, Y. S., Howard, C. B., Raftery, L. J., Mahler, S. M., Wang, Y., & Trau, M. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02216 · Cited by 81
Diffusing protein binders to intrinsically disordered proteins
Liu, C., Wu, K., Choi, H., Han, H. L., Zhang, X., Watson, J. L., Ahn, G., Zhang, J. Z., Shijo, S., Good, L. L., et al. (2025) · Nature · doi:10.1038/s41586-025-09248-9 · Cited by 79
Schneider, E. H., & Seifert, R. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.05.004 · Cited by 78
Guidelines for authors and reviewers on antibody use in physiology studies
Brooks, H. L., & Lindsey, M. L. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00512.2017 · Cited by 78
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Tiambeng, T. N., Roberts, D. S., Brown, K. A., Zhu, Y., Chen, B., Wu, Z., Mitchell, S. D., Guardado-Alvarez, T. M., Jin, S., & Ge, Y. (2020) · Nature Communications · doi:10.1038/s41467-020-17643-1 · Cited by 76
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Matsunaga, K., Kimoto, M., Hanson, C. A., Sanford, M. E., Young, H. A., & Hirao, I. (2015) · Scientific Reports · doi:10.1038/srep18478 · Cited by 76
Aloia, A., Petrova, E., Tomiuk, S., Bissels, U., Déas, O., Saini, M., Zickgraf, F. M., Wagner, S., Spaich, S., Sütterlin, M., et al. (2015) · Breast Cancer Research · doi:10.1186/s13058-015-0652-6 · Cited by 75
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de Lima, W. C., Gasteiger, E., Marcatili, P., Duek, P. D., Bairoch, A., & Cosson, P. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz714 · Cited by 70
Hu, Z., Zhou, X., Duan, J., Wu, X., Wu, J., Zhang, P., Liang, W., Guo, J., Cai, H., Sun, P., et al. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.129640 · Cited by 69
Wiśniewski, J. R., & Mann, M. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00403 · Cited by 71
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Delhalle, S., Bode, S. F. N., Balling, R., Ollert, M. W., & HeFeng, F. Q. (2018) · npj Systems Biology and Applications · doi:10.1038/s41540-017-0045-9 · Cited by 70
Dickey, D. D., & Giangrande, P. H. (2015) · Methods · doi:10.1016/j.ymeth.2015.11.020 · Cited by 66
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Beslic, D., Tscheuschner, G., Renard, B. Y., Weller, M. G., & Muth, T. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac542 · Cited by 65
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Vandemoortele, G., Eyckerman, S., & Gevaert, K. (2019) · Trends in biotechnology · doi:10.1016/j.tibtech.2019.03.016 · Cited by 65
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Voskuil, J. L. A. (2017) · F1000Research · doi:10.12688/f1000research.10851.1 · Cited by 66
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Venkataraman, A., Yang, K., Irizarry, J., Mackiewicz, M., Mita, P., Kuang, Z., Lin, X., Ghosh, D., Liu, S., Ramos, P., et al. (2018) · Nature Methods · doi:10.1038/nmeth.4632 · Cited by 62
Li, P., Pang, J., Xu, S., He, H., Ma, Y., & Liu, Z. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202113528 · Cited by 62
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van der Burgt, Y. E. M., Kilgour, D. P. A., Tsybin, Y. O., Srzentić, K., Fornelli, L., Beck, A., Wuhrer, M., & Nicolardi, S. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04515 · Cited by 62
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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