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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77-90% of biomedical experiments are not reproducible.
“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]
The opening section (page unavailable) reports that a study replicated results from only 6 of 53 landmark preclinical studies—about 89% were not replicated. That supports a figure within the claimed range, but the paper does not give the 77% figure or establish that 77–90% of biomedical experiments generally are not reproducible. (LLM, conf=0.88)
Experimental — accuracy not yet measuredSequence-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.
“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
The “TWO STEPS” section says sequence-defined, recombinant antibodies would let researchers use the same binding reagents under the same conditions. “WILDLY VARIABLE” describes animal-serum-derived polyclonal antibodies as mixtures whose functionality varies between batches. The paper supports this comparison for antibodies, but does not establish it for products purified from animal tissues or biological fluids generally, or describe those products as chemically undefined. (LLM, conf=0.86)
Experimental — accuracy not yet measuredAntibodies have limitations including batch-to-batch variation, high production cost, poor chemical stability, and lack of proteoform-specific epitope recognition, which contribute to reproducibility issues.
“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]
Antibody-based platforms suffer from significant limitations including batch-to-batch variability, high cost of antibody production, and relatively low chemical stability.
“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]
These NPs can serve as replacements to conventional immuno-based techniques to overcome antibody-related limitations in cTnI immunoassays and potentially address the current reproducibility crisis caused by antibodies in general.
“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]
The NP-Pep is capable of reproducibly and effectively enriching cTnI across all tested serum samples without the use of antibody.
“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]
The functionalized NPs possess unique advantages over antibody-based platforms: comparable size and diffusion kinetics to proteins, high surface area per volume and high number of flexible binding sites, and inexpensive, simple, fast, scalable synthesis with minimal batch-to-batch variability.
“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]
The 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.
“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
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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 · see citing works
Raise standards for preclinical cancer research
Begley, C. G., & Ellis, L. M. (2012) · Nature · doi:10.1038/483531a · Cited by 2,979 · see citing works
Policy: NIH plans to enhance reproducibility
Collins, F. S., & Tabak, L. A. (2014) · Nature · doi:10.1038/505612a · Cited by 1,247 · see citing works
Engineering novel binding proteins from nonimmunoglobulin domains
Binz, H. K., Amstutz, P., & Plückthun, A. (2005) · Nature Biotechnology · doi:10.1038/nbt1127 · Cited by 676 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 114 · see citing works
Commercial antibodies and their validation
Voskuil, J. L. A. (2014) · F1000Research · doi:10.12688/f1000research.4966.2 · Cited by 82 · see citing works
Commercial antibodies and their validation
Voskuil, J. (2014) · F1000Research · doi:10.12688/f1000research.4966.1 · Cited by 82 · see citing works
Multiplexed immuno‐precipitation with 1725 commercially available antibodies to cellular proteins
Slåstad, H., Wu, W., Goullart, L., Kanderová, V., Tjønnfjord, G. E., Stuchlý, J., Kalina, T., Holm, A., & Lund‐Johansen, F. (2011) · PROTEOMICS · doi:10.1002/pmic.201000744 · Cited by 28 · see citing works
Flagged first, then by citations
Research works printed but not linked: 3
- Vasilevsky, N. A. et al. PeerJ 1, e148 (2013).
- Voskuil, J. L. A. F1000Research 3, 232 (2014).
- Gold, L. et al. Cold Spring Harb. Perspect. Biol. 4, a003582 (2012).
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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 975 · see citing works
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 · see citing works
Reproducibility crisis: Blame it on the antibodies
Baker, M. (2015) · Nature · doi:10.1038/521274a · Cited by 830 · see citing works
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 · see citing works
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 554 · see citing works
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 552 · see citing works
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 · see citing works
Stein, C. (2015) · Annual Review of Medicine · doi:10.1146/annurev-med-062613-093100 · Cited by 493 · see citing works
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 435 · see citing works
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 414 · see citing works
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 · see citing works
Switchable Fluorophores for Single-Molecule Localization Microscopy
Li, H., & Vaughan, J. C. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00767 · Cited by 311 · see citing works
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 · see citing works
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 265 · see citing works
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 · see citing works
Soh, J. H., Chan, H., & Ying, J. Y. (2020) · Nano Today · doi:10.1016/j.nantod.2019.100831 · Cited by 231 · see citing works
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 230 · see citing works
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 220 · see citing works
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 203 · see citing works
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 · see citing works
Novel Strategies to Address the Challenges in Top-Down Proteomics
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 191 · see citing works
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 · see citing works
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 175 · see citing works
New concepts in opioid analgesia
Stein, C. (2018) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2018.1516204 · Cited by 175 · see citing works
Platforms for Single-Cell Collection and Analysis
Valihrach, L., Androvic, P., & Kubista, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030807 · Cited by 165 · see citing works
Unpicking the proteome in single cells
Slavov, N. (2020) · Science · doi:10.1126/science.aaz6695 · Cited by 162 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 154 · see citing works
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Coutu, D. L., Kokkaliaris, K. D., Kunz, L., & Schroeder, T. (2017) · Nature Biotechnology · doi:10.1038/nbt.4006 · Cited by 151 · see citing works
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 149 · see citing works
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 · see citing works
Overlooked Benefits of using Polyclonal Antibodies
Ascoli, C. A., & Aggeler, B. (2018) · BioTechniques · doi:10.2144/btn-2018-0065 · Cited by 142 · see citing works
Animal immunization, in vitro display technologies, and machine learning for antibody discovery
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 157 · see citing works
Antibody anarchy: A call to order
Baker, M. (2015) · Nature · doi:10.1038/527545a · Cited by 140 · see citing works
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 139 · see citing works
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 137 · see citing works
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 · see citing works
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 136 · see citing works
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 134 · see citing works
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 · see citing works
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 127 · see citing works
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 · see citing works
Bauer, M., Strom, M., Hammond, D., & Shigdar, S. L. (2019) · Molecules · doi:10.3390/molecules24234377 · Cited by 119 · see citing works
Quality Issues of Research Antibodies
Weller, M. G. (2016) · Analytical Chemistry Insights · doi:10.4137/aci.s31614 · Cited by 117 · see citing works
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 · see citing works
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 115 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 109 · see citing works
An improved yeast surface display platform for the screening of nanobody immune libraries
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 109 · see citing works
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 111 · see citing works
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 108 · see citing works
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 108 · see citing works
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 · see citing works
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 108 · see citing works
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 107 · see citing works
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 · see citing works
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 104 · see citing works
Analytical techniques for multiplex analysis of protein biomarkers
van Gool, A. V., Corrales, F., Čolović, M., Krstić, D., Oliver-Martos, B., Martínez-Cáceres, E., Jakaša, I., Gajski, G., Brun, V., Kyriacou, K., et al. (2020) · Espert Review of Proteomics · doi:10.1080/14789450.2020.1763174 · Cited by 94 · see citing works
Reproducibility2020: Progress and priorities
Freedman, L. P., Venugopalan, G., & Wisman, R. (2017) · F1000Research · doi:10.12688/f1000research.11334.1 · Cited by 102 · see citing works
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 102 · see citing works
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 101 · see citing works
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 · see citing works
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Chan, A. C., Martyn, G. D., & Carter, P. J. (2025) · Nature reviews. Immunology · doi:10.1038/s41577-025-01207-9 · Cited by 96 · see citing works
Klotho: An Elephant in Aging Research
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 · see citing works
Parola, C., Neumeier, D., & Reddy, S. T. (2017) · Immunology · doi:10.1111/imm.12838 · Cited by 91 · see citing works
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 · see citing works
Developments and Applications of Functional Protein Microarrays
Syu, G., Dunn, J., & Zhu, H. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r120.001936 · Cited by 90 · see citing works
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 · see citing works
Chiron, C., Tompkins, T. A., & Burguière, P. (2017) · Journal of Applied Microbiology · doi:10.1111/jam.13666 · Cited by 85 · see citing works
Butler, T. A. J., Paúl, J., Chan, E., Smith, R., & Tolosa, J. M. (2019) · BioMed Research International · doi:10.1155/2019/5214821 · Cited by 85 · see citing works
Antibody Validation by Western Blotting
Signore, M., Manganelli, V., & Hodge, A. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6990-6_4 · Cited by 84 · see citing works
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 · see citing works
Generation of Murine Monoclonal Antibodies by Hybridoma Technology
Holzlöhner, P., & Hanack, K. (2017) · Journal of Visualized Experiments · doi:10.3791/54832 · Cited by 81 · see citing works
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 · see citing works
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 · see citing works
Schneider, E. H., & Seifert, R. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.05.004 · Cited by 78 · see citing works
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 · see citing works
Accounting for Protein Subcellular Localization: A Compartmental Map of the Rat Liver Proteome
Jadot, M., Boonen, M., Thirion, J., Wang, N., Xing, J., Zhao, C., Tannous, A., Qian, M., Zheng, H., Everett, J. K., et al. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.064527 · Cited by 77 · see citing works
Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum
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 · see citing works
Architecture of high-affinity unnatural-base DNA aptamers toward pharmaceutical applications
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 · see citing works
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 74 · see citing works
Deep sequencing in library selection projects: what insight does it bring?
Glanville, J., D’Angelo, S., Khan, T. A., Reddy, S. T., Naranjo, L. A., Ferrara, F., & Bradbury, A. M. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.09.001 · Cited by 71 · see citing works
Self-citationThe ABCD database: a repository for chemically defined antibodies
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 · see citing works
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 · see citing works
Wiśniewski, J. R., & Mann, M. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00403 · Cited by 69 · see citing works
A roadmap towards personalized immunology
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 66 · see citing works
Dickey, D. D., & Giangrande, P. H. (2015) · Methods · doi:10.1016/j.ymeth.2015.11.020 · Cited by 65 · see citing works
Comprehensive evaluation of peptide de novo sequencing tools for monoclonal antibody assembly
Beslic, D., Tscheuschner, G., Renard, B. Y., Weller, M. G., & Muth, T. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac542 · Cited by 65 · see citing works
Pick a Tag and Explore the Functions of Your Pet Protein
Vandemoortele, G., Eyckerman, S., & Gevaert, K. (2019) · Trends in biotechnology · doi:10.1016/j.tibtech.2019.03.016 · Cited by 64 · see citing works
The challenges with the validation of research antibodies
Voskuil, J. L. A. (2017) · F1000Research · doi:10.12688/f1000research.10851.1 · Cited by 64 · see citing works
A toolbox of immunoprecipitation-grade monoclonal antibodies to human transcription factors
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 · see citing works
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 · see citing works
Mechanically stimulated ATP release from mammalian cells: systematic review and meta-analysis
Mikolajewicz, N., Mohammed, A., Morris, M., & Komarova, S. V. (2018) · Journal of Cell Science · doi:10.1242/jcs.223354 · Cited by 62 · see citing works
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 · see citing works
- 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 · 2014: 1
- 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
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › 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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