ArticleJournal of molecular biology2012
Broad ranges of affinity and specificity of anti-histone antibodies revealed by a quantitative peptide immunoprecipitation assay.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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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
51 citing papers in PubMed.
- Lactate metabolism and lactylation in female reproductive diseases: From metabolic rewiring to biomarkers and translational therapeutics.Clinical and translational medicine · 2026Review
- Histone Modifications in Cardiovascular Disease: Mechanisms and Therapeutic Opportunities.MedComm · 2026Review
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- Lactylation in cancer: molecular mechanisms and advances in clinical study.Molecular cancer · 2026Review
- Review
- Engineering antibody-drug conjugates targeting an adhesion GPCR, CD97.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Binding mode-guided development of high-performance antibodies targeting site-specific posttranslational modifications.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Beyond the tail: the consequence of context in histone post-translational modification and chromatin research.The Biochemical journal · 2024Article
- An Optimized and High-Throughput Method for Histone Propionylation and Data-Independent Acquisition Analysis for the Identification and Quantification of Histone Post-translational Modifications.Journal of the American Society for Mass Spectrometry · 2023Article
- Monobody Inhibitor Selective to the Phosphatase Domain of SHP2 and its Use as a Probe for Quantifying SHP2 Allosteric Regulation.Journal of molecular biology · 2023Article
- High-affinity chromodomains engineered for improved detection of histone methylation and enhanced CRISPR-based gene repression.Nature communications · 2022Article
- High-valency Anti-CD99 Antibodies Toward the Treatment of T Cell Acute Lymphoblastic Leukemia.Journal of molecular biology · 2022Article
- Modified Histone Peptides Linked to Magnetic Beads Reduce Binding Specificity.International journal of molecular sciences · 2022Article
- Covalent Chemical Tools for Profiling Post-Translational Modifications.Frontiers in chemistry · 2022Review
- Article
- Multiplex bead binding assays using off-the-shelf components and common flow cytometers.Journal of immunological methods · 2021Article
- The ACE2-binding Interface of SARS-CoV-2 Spike Inherently Deflects Immune Recognition.Journal of molecular biology · 2021Article
- High-specificity antibodies and detection methods for quantifying phosphorylated tau from clinical samples.Antibody therapeutics · 2021Review
- Chromatin Immunoprecipitation (ChIP) to Study DNA-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2021Article
- A physical basis for quantitative ChIP-sequencing.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Antibodies directed against histone posttranslational modifications (PTMs) are critical tools in epigenetics research, particularly in the widely used chromatin immunoprecipitation (ChIP) experiments. However, a lack of quantitative methods for characterizing such antibodies has been a major bottleneck in accurate and reproducible analysis of histone modifications. Here, we report a simple and sensitive method for quantitatively characterizing polyclonal and monoclonal antibodies for histone PTMs in a ChIP-like format. Importantly, it determines the apparent dissociation constants for the interactions of an antibody with peptides harboring cognate or off-target PTMs. Analyses of commercial antibodies revealed large ranges of affinity, specificity and binding capacity as well as substantial lot-to-lot variations, suggesting the importance of quantitatively characterizing each antibody intended to be used in ChIP experiments and optimizing experimental conditions accordingly. Furthermore, using this method, we identified additional factors potentially affecting the interpretation of ChIP experiments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.