{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang Y"],"funding":["National Institutes of Health","NIGMS NIH HHS"],"pagination":["e202300081"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11081099"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["63(10-11)"],"pubmed_abstract":["Truncated mucin-type O-glycans, such as Tn-associated antigens, are aberrantly expressed biomarkers of cancer, but remain challenging to target. Reactive antibodies to these antigens either lack high-affinity or are prone to antigen escape. Here, we have developed a robust chemoenzymatic strategy for the global labeling of Tn-associated antigens, i.e. Tn (GalNAcα-O-Ser/Thr), Thomsen-Friedenreich (Galβ1-3GalNAcα-O-Ser/Thr, TF) and STF (Neu5Acα2-3Galβ1-3GalNAcα-O-Ser/Thr, STF) antigens, in human whole blood with high efficiency and selectivity. This method relies on the use of the O-glycan sialyltransferase ST6GalNAc1 to transfer a sialic acid-functionalized adaptor to the GalNAc residue of these antigens. By tagging, the adaptor functionalized antigens can be easily targeted by customized s"],"journal":["Israel journal of chemistry"],"pubmed_title":["Chemoenzymatic Tagging of Tn/TF/STF Antigens in Living Systems."],"pmcid":["PMC11081099"],"funding_grant_id":["P41 GM103390","R35 GM139643","P01GM107012","R01GM117145","R01 GM130915","U01 GM120408","U01GM120408","R01GM130915","P01 GM107012","P41 GM103390","R01 GM117145","R35GM139643"],"pubmed_authors":["Yang JY","Gao B","Sharpless KB","Wu M","Chen M","Young TS","Chapla DG","Wu P","Cappiello JR","Moremen KW","Liu Y","Yang Y","Yu C","Li JP","Hong S"],"additional_accession":[]},"is_claimable":false,"name":"Chemoenzymatic Tagging of Tn/TF/STF Antigens in Living Systems.","description":"Truncated mucin-type O-glycans, such as Tn-associated antigens, are aberrantly expressed biomarkers of cancer, but remain challenging to target. Reactive antibodies to these antigens either lack high-affinity or are prone to antigen escape. Here, we have developed a robust chemoenzymatic strategy for the global labeling of Tn-associated antigens, i.e. Tn (GalNAcα-O-Ser/Thr), Thomsen-Friedenreich (Galβ1-3GalNAcα-O-Ser/Thr, TF) and STF (Neu5Acα2-3Galβ1-3GalNAcα-O-Ser/Thr, STF) antigens, in human whole blood with high efficiency and selectivity. This method relies on the use of the O-glycan sialyltransferase ST6GalNAc1 to transfer a sialic acid-functionalized adaptor to the GalNAc residue of these antigens. By tagging, the adaptor functionalized antigens can be easily targeted by customized s","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Oct","modification":"2025-04-04T01:03:21.056Z","creation":"2025-04-04T01:03:21.056Z"},"accession":"S-EPMC11081099","cross_references":{"pubmed":["38737670"],"doi":["10.1002/ijch.202300081"]}}