TMT Labeling Steps

The chemical structure of TMT tags consists of a reporter group, a balance group, and a peptide reactive group. Essentially, they are isobaric tags with equal relative molecular masses, available in 2, 6, 10, or 16-plex formats. These isobaric tags can contain up to 16 different relative molecular mass reporter and balance groups, currently achieving up to 16-plex TMT.

TMT reagents efficiently label digested peptides through the reactive group, forming covalent bonds with the N-terminal and lysine side chain amino groups of peptides, achieving peptide sample labeling. TMT labeling steps: Protein samples are digested into small peptide fragments by trypsin, then labeled with different TMT reagents for different samples. The labeled samples are then mixed in equal amounts for mass spectrometry analysis. In mass spectrometry, the same peptide from different samples carries different reporter groups, which produce reporter ions of different molecular masses upon fragmentation in MS/MS. The signal intensity of reporter ions in mass spectrometry represents the relative abundance of peptides in different samples, enabling relative quantification analysis of proteins across different samples.

Biotech company Baitaike uses the Thermo Fisher Orbitrap Fusion Lumos mass spectrometry platform combined with nanoLC-MS/MS nano-scale chromatography technology to provideTMT-based proteomics analysisservices. The Orbitrap Fusion Lumos mass spectrometer is currently the highest resolution and sensitivity mass spectrometer, ensuring sensitivity in identifying low-abundance peptide fragments. During peptide fragmentation, it employs a combination of HCD and ETD modes to ensure the integrity of peptide fragments. You only need to send your samples and inform us of your experimental objectives, and we will handle all subsequent project matters.

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