{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Guo Y"],"funding":["NIGMS NIH HHS"],"pagination":["101873"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9587358"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9"],"pubmed_abstract":["Isobaric chemical tag labeling for quantification of intact proteins in complex samples is limited due to the tendency of intact proteins precipitate under labeling conditions and increased sample complexity as a result of side products (<i>i.e.</i>, incomplete labeling or labeling of unintended residues). To reduce precipitation under labeling conditions, we developed a technique to remove large proteoforms that allowed for the labeling and characterization of small proteoforms (<35 kDa) using top-down proteomics. We also systematically optimized protein-level Tandem Mass Tag (TMT) labeling conditions to obtain optimal labeling parameters for complex samples. Here, we present a benchmarking protocol for protein-level TMT labeling for quantitative top-down proteomics, including complex int"],"journal":["MethodsX"],"pubmed_title":["A benchmarking protocol for intact protein-level Tandem Mass Tag (TMT) labeling for quantitative top-down proteomics."],"pmcid":["PMC9587358"],"funding_grant_id":["R01 GM118470"],"pubmed_authors":["Cupp-Sutton KA","Liu X","Guo Y","Wu S","Yu D"],"additional_accession":[]},"is_claimable":false,"name":"A benchmarking protocol for intact protein-level Tandem Mass Tag (TMT) labeling for quantitative top-down proteomics.","description":"Isobaric chemical tag labeling for quantification of intact proteins in complex samples is limited due to the tendency of intact proteins precipitate under labeling conditions and increased sample complexity as a result of side products (<i>i.e.</i>, incomplete labeling or labeling of unintended residues). To reduce precipitation under labeling conditions, we developed a technique to remove large proteoforms that allowed for the labeling and characterization of small proteoforms (<35 kDa) using top-down proteomics. We also systematically optimized protein-level Tandem Mass Tag (TMT) labeling conditions to obtain optimal labeling parameters for complex samples. Here, we present a benchmarking protocol for protein-level TMT labeling for quantitative top-down proteomics, including complex int","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-05-28T01:20:16.346Z","creation":"2025-02-18T23:29:48.653Z"},"accession":"S-EPMC9587358","cross_references":{"pubmed":["36281278"],"doi":["10.1016/j.mex.2022.101873"]}}