Tandem Mass Tag™ (TMT) Systems
The Thermo Scientific™ Tandem Mass Tag™ Reagents are designed to enable identification and quantitation of proteins in different samples using tandem mass spectrometry (MS). The TMT10plex Label Reagents share an identical structure with TMTzero, TMTduplex, and TMTsixplex Reagents but contain different numbers and combinations of 13C and 15N isotopes in the mass reporter.
- Powerful—concurrent MS analysis of multiple samples increases sample throughput and enables relative quantitation of up to 10 different samples derived from cells, tissues or biological fluids
- Consistent—identical reagent structure and performance among TMTzero, TMTduplex, TMTsixplex and TMT10plex Reagents allow efficient transition from method development to multiplex quantitation
- Robust—increased multiplex capability results in fewer missing quantitative values
- Flexible—multiple chemistries allow functional group specific labeling and enrichment, using anti-TMT immobilized resin.
- Efficient—amine-, cysteine- and carbonyl-reactive chemistries utilize an effective strategy for efficient labeling of target functional group
- Compatible—optimized for use with high-resolution MS/MS platforms using SP2 or SPS MS3 quantitation mode with data analysis fully supported by Thermo Scientific™ Proteome Discoverer™ 2.1 Software
Choose the right TMT product for your applications
|Reactive chemistry||Amine-reactive mass tags||Amine-reactive mass tags||Amine-reactive mass tags||Cysteine-reactive mass tags||Carbonyl-reactive mass tags|
|Formats||Labeling reagents & kits||Labeling reagents & kits||Labeling reagents & kits||Labeling reagents & kits||Labeling reagents only|
|Standard packaging||0.8 mg/vial||0.8 and 5 mg/vial||0.8 and 5 mg/vial||0.2 mg/vial||0.2 mg/vial|
Procedure summary for MS experiments with Thermo Scientific™ TMT10plex Isobaric Mass Tagging Reagents. Protein extracts isolated from cells or tissues are reduced, alkylated and digested overnight. Samples are labeled with the TMT Reagents and then mixed before sample fractionation and clean up. Labeled samples are analyzed by high-resolution Orbitrap LC-MS/MS before data analysis to identify peptides and quantify reporter ion relative abundance.
Measured induction of S-nitrosylation in phosphoglycerate kinase 1 peptide. BV-2 glioma cells were either untreated or treated with lipopolysaccharide (LPS) or S-nitrosocysteine (SNOC) for 20 hours to induce S-nitrosylation and selectively labeled with iodoTMTsixplex Reagents using the S-nitrosylation switch assay. MS spectrum includes phosphoglycerate kinase 1 peptide (GcITIIGGGDTATccAK, inset) showing localization of the iodoTMT-modified cysteine (red). Inserted graph shows an increase in S-nitrosylation of phosphoglycerate kinase 1 peptide in response to S-nitrosylation inducing agents lipopolysaccharide (LPS, 127 & 130) and S-nitrosocysteine (SNOC, 129 &131) determined by relative quantitation of TMT reporter ions in duplicate samples.
Video of TMT10plex reagents in action
Additional mass spec products
For Research Use Only. Not for use in diagnostic procedures.