ArticleNature protocols2014
Generation and purification of highly specific antibodies for detecting post-translationally modified proteins in vivo.
Article in Nature protocols, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
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- Advances in protein dot blot: principles, technical specifics, applications, and future perspectives.Frontiers in molecular biosciences · 2026Review
- Mitochondrial stress orchestrates chromatin remodeling and longevity via phosphoregulation of the NuRD component LIN-40.Science China. Life sciences · 2025Article
- Epitope binning for multiple antibodies simultaneously using mammalian cell display and DNA sequencing.Communications biology · 2024Article
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- GRAF1 integrates PINK1-Parkin signaling and actin dynamics to mediate cardiac mitochondrial homeostasis.Nature communications · 2023Article
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- Monoclonal antibodies to activated CDK4: use to investigate normal and cancerous cell cycle regulation and involvement of phosphorylations of p21 and p27.Cell cycle (Georgetown, Tex.) · 2022Article
- Epitope-directed monoclonal antibody production using a mixed antigen cocktail facilitates antibody characterization and validation.Communications biology · 2021Article
- Isoelectric Focusing to Quantify Rhodopsin Phosphorylation in Mouse Retina.Bio-protocol · 2019Article
- Collaborative Control of Cell Cycle Progression by the RNA Exonuclease Dis3 and Ras Is Conserved Across Species.Genetics · 2016Article
- Novel method for the high-throughput production of phosphorylation site-specific monoclonal antibodies.Scientific reports · 2016Article
- Site-selective protein-modification chemistry for basic biology and drug development.Nature chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Post-translational modifications alter protein structure, affecting activity, stability, localization and/or binding partners. Antibodies that specifically recognize post-translationally modified proteins have a number of uses including immunocytochemistry and immunoprecipitation of the modified protein to purify protein-protein and protein-nucleic acid complexes. However, antibodies directed at modified sites on individual proteins are often nonspecific. Here we describe a protocol to purify polyclonal antibodies that specifically detect the modified protein of interest. The approach uses iterative rounds of subtraction and affinity purification, using stringent washes to remove antibodies that recognize the unmodified protein and low sequence complexity epitopes containing the modified amino acid. Dot blot and western blot assays are used to assess antibody preparation specificity. The approach is designed to overcome the common occurrence that a single round of subtraction and affinity purification is not sufficient to obtain a modified protein-specific antibody preparation. One full round of antibody purification and specificity testing takes 6 d of discontinuous time.
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Registered trials
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