{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["97(41)"],"submitter":["Liu PK"],"pubmed_abstract":["Isobaric labeling techniques are widely used in mass spectrometry-based quantitative proteomics to enable the simultaneous analysis of multiple samples. However, commercial isobaric tags are expensive due to complex synthesis and costly reagents, limiting their use in large-scale studies. Here, we introduce a novel, cost-effective diethylalanine-based isobaric reagent (DeAla), synthesized using diethylated alanine and β-alanine with <i>N</i>-hydroxysuccinimide. The DeAla tag offers several advantages, including improved peptide fragmentation, enhanced protein identification, and competitive pricing. We optimized labeling efficiency and collision energy parameters, demonstrating that DeAla-labeled peptides produce more backbone fragmentation ions and higher XCorr values compared to peptides"],"journal":["Analytical chemistry"],"pagination":["22643-22650"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12547851"],"repository":["biostudies-literature"],"pubmed_title":["13-Plex DeAla Isobaric Reagents for High-Throughput Proteome Quantification."],"pmcid":["PMC12547851"],"pubmed_authors":["Nassar A","Gu TJ","Wang D","Xu S","Wang Z","Li L","Liu PK","Chiang HY"],"additional_accession":[]},"is_claimable":false,"name":"13-Plex DeAla Isobaric Reagents for High-Throughput Proteome Quantification.","description":"Isobaric labeling techniques are widely used in mass spectrometry-based quantitative proteomics to enable the simultaneous analysis of multiple samples. However, commercial isobaric tags are expensive due to complex synthesis and costly reagents, limiting their use in large-scale studies. Here, we introduce a novel, cost-effective diethylalanine-based isobaric reagent (DeAla), synthesized using diethylated alanine and β-alanine with <i>N</i>-hydroxysuccinimide. The DeAla tag offers several advantages, including improved peptide fragmentation, enhanced protein identification, and competitive pricing. We optimized labeling efficiency and collision energy parameters, demonstrating that DeAla-labeled peptides produce more backbone fragmentation ions and higher XCorr values compared to peptides","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-04T16:22:14.11Z","creation":"2026-06-02T03:08:00.462Z"},"accession":"S-EPMC12547851","cross_references":{"pubmed":["41053940"],"doi":["10.1021/acs.analchem.5c03910"]}}