iTRAQ/TMT Labeled Peptide Segments
The application of iTRAQ or TMT labeling technologies is a widely used approach in quantitative proteomics analysis. These methods are based on stable isotope labeling, where isotope tags are chemically introduced to the amino groups at the N-terminus and lysine (K) side chains of peptides. This modification assigns each peptide a distinct mass tag, which can be identified during mass spectrometry analysis. Both iTRAQ and TMT are chemical labeling techniques that enable isotopic labeling of peptides, thereby facilitating accurate quantification of peptides and proteins.
iTRAQ Labeling
iTRAQ (Isobaric Tags for Relative and Absolute Quantitation) is a quantitative proteomics technique that utilizes isotopic labeling to simultaneously measure protein expression across 2-8 samples. The iTRAQ reagent consists of a balanced chemical tag, comprising an activated ester for peptide binding, a reporter group that provides a distinct mass-to-charge signal, and a neutral moiety for balance. This labeling allows for the identification of reporter ions corresponding to different samples in the MS/MS spectra.
TMT Labeling
TMT (Tandem Mass Tag) functions similarly to iTRAQ as an isotopic labeling strategy in proteomics, with distinctions in label structure and reporter ions used in mass spectrometry. TMT tags consist of an imine-activated ester, a mass-to-charge reporter group, and a neutral balancing moiety, enabling the labeling of 2-16 samples to yield unique reporter ions in MS/MS spectra.
Applications
The employment of iTRAQ or TMT labeling provides researchers with precise tools to compare protein expression levels, both absolute and relative, across different samples. These methods are extensively applied in proteomics research, aiding in disease diagnosis, drug target discovery, and elucidation of biological mechanisms.
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