ArticleProteomics2016
Commercially available antibodies can be applied in quantitative multiplexed peptide immunoaffinity enrichment targeted mass spectrometry assays.
Article in Proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Quantification of total sBCMA in human plasma by peptide-level immunocapture LC-MS/MS.Journal of mass spectrometry and advances in the clinical lab · 2025Article
- Targeted mass spectrometry-based assays enable multiplex quantification of receptor tyrosine kinase, MAP Kinase, and AKT signaling.Cell reports methods · 2021Article
- An Introduction to Advanced Targeted Acquisition Methods.Molecular & cellular proteomics : MCP · 2021Review
- Immunocapture sample clean-up in determination of low abundant protein biomarkers - a feasibility study of peptide capture by anti-protein antibodies.RSC advances · 2019Article
- Clinical potential of mass spectrometry-based proteogenomics.Nature reviews. Clinical oncology · 2019Review
- Personalized Proteomics: The Future of Precision Medicine.Proteomes · 2016Article
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Authors and funding
9 authors.
Funding
Abstract
Immunoaffinity enrichment of peptides coupled to multiple reaction monitoring-mass spectrometry (immuno-MRM) enables highly specific, sensitive, and precise quantification of peptides and post-translational modifications. Major obstacles to developing a large number of immuno-MRM assays are poor availability of monoclonal antibodies (mAbs) validated for immunoaffinity enrichment of peptides and the cost and lead time of developing the antibodies de novo. Although many thousands of mAbs are commercially offered, few have been tested for application to immunoaffinity enrichment of peptides. In this study, we tested the success rate of using commercially available mAbs for peptide immuno-MRM assays. We selected 105 commercial mAbs (76 targeting non-modified "pan" epitopes, 29 targeting phosphorylation) to proteins associated with the DNA damage response network. We found that 8 of the 76 pan (11%) and 5 of the 29 phospho-specific mAbs (17%) captured tryptic peptides (detected by LC-MS/MS) of their protein targets from human cell lysates. Seven of these mAbs were successfully used to configure and analytically characterize immuno-MRM assays. By applying selection criteria upfront, the results indicate that a screening success rate of up to 24% is possible, establishing the feasibility of screening a large number of catalog antibodies to provide readily-available assay reagents.
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Registered trials
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