TMT 18plex
TMT 18plex is a high-throughput protein quantification technique based on tandem mass tag (TMT) technology, enabling the simultaneous relative quantification of up to 18 samples within a single experiment. TMT technology employs a chemical labeling strategy in which isotope-coded tags are covalently attached to the N-terminus or lysine residues of peptides, facilitating the distinction and quantification of proteins from different samples during mass spectrometry analysis. The introduction of TMT 18plex has significantly enhanced the throughput of proteomics research, allowing for comparative analyses of protein expression across multiple biological samples under standardized experimental conditions, thereby improving data stability and comparability. Due to its superior efficiency and precision, TMT 18plex is extensively utilized in various research fields, including disease biomarker discovery, cell signaling pathway analysis, drug target identification, as well as biomedical and biotechnological investigations. For instance, in disease-related studies, this technique enables the simultaneous analysis of protein expression levels across multiple patient and control samples within the same experimental batch, thereby enhancing the reliability of biomarker screening. In cell biology, TMT 18plex facilitates the monitoring of dynamic protein expression changes under different experimental conditions, such as drug treatments, metabolic regulation, or immune responses. Moreover, in integrative multi-omics research, this method can be integrated with transcriptomics and metabolomics to provide a comprehensive biological perspective, thereby elucidating complex molecular regulatory networks.
The fundamental principle of TMT 18plex relies on isotope-coded chemical tags that exhibit nearly identical masses across different samples but generate distinct reporter ions upon fragmentation under collision-induced dissociation (CID) or high-energy collision dissociation (HCD) conditions, thereby enabling precise quantitative analysis. Each TMT tag comprises a reporter ion group, a normalization group, and an amine-reactive group, ensuring specific labeling of peptides generated via enzymatic digestion. In mass spectrometry analysis, all labeled peptides appear as identical mass peaks in first-stage mass spectrometry (MS1), whereas the distinct reporter ions released in second-stage mass spectrometry (MS2) allow for quantification. Compared with conventional protein quantification approaches, such as label-free quantification or isobaric tags for relative and absolute quantification (iTRAQ), TMT 18plex offers significant advantages in terms of data consistency, quantification accuracy, and sample throughput.
Despite the superior throughput and accuracy of TMT 18plex, its implementation presents several challenges. This technique requires advanced mass spectrometry instrumentation and rigorous sample preparation protocols, particularly for large-scale data processing, where optimized algorithms are necessary to minimize quantification bias. Additionally, as TMT 18plex quantification relies on reporter ion intensities, peptide co-isolation in complex samples may introduce signal interference, compromising quantification accuracy. To address this issue, optimizing mass spectrometry acquisition strategies, such as synchronous precursor selection (SPS-MS3), can effectively mitigate co-isolation effects and enhance quantitative precision. Furthermore, the relatively high cost of TMT 18plex necessitates careful experimental design in large-scale studies to maximize data utilization efficiency.
MtoZ Biolabs is dedicated to delivering high-quality proteomic analytical services. By leveraging cutting-edge proteomics technologies, we provide high-throughput and high-precision protein quantification solutions to support disease research, biomarker discovery, and drug target identification.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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