Our TMT proteome profiling service characterizes changes in protein expression proteome-wide, with the depth and precision to detect both large and subtle differences between samples.
At a glance
- More than 9,500 proteins and 100,000 peptides quantified
- More than 2 million quantitative measurements per study
- TMT 18-plex: up to 18 samples measured together
- Suited to degradation profiling, biomarker discovery and large cohort studies, in cell lines, tissues and biofluids
How it works
Proteins are extracted from up to 18 samples, digested and labeled with TMT isobaric barcodes. The samples are mixed and analyzed together in a single LC-MS run on Orbitrap instruments, with quantification by SPS MS3 using real-time search.
Example data: six cancer cell lines
Six cancer cell lines (H358, HCT-116, HEK293, HeLa, Jurkat and Panc-1) were each prepared in triplicate and analyzed together. The study quantified 9,562 protein groups and 127,149 peptides with no missing values. Differences between cell lines dominate, while replicates agree closely, with an average coefficient of variation below 5%. Measurements span more than five orders of magnitude and capture changes greater than 60-fold.
Spotlight: individual proteins
Individual proteins show both large and subtle differences between cell lines. FOLR1 is strongly expressed in HeLa cells, RASF2 in HEK293 and Jurkat cells, and B3A2 varies more modestly, highest in Panc-1. Close agreement between replicates and the absence of missing values make these differences straightforward to interpret.
