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Analysis of the plasma proteome using iTRAQ and TMT‐based Isobaric labeling
Author(s) -
Moulder Robert,
Bhosale Santosh D.,
Goodlett David R.,
Lahesmaa Riitta
Publication year - 2017
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/mas.21550
Subject(s) - isobaric labeling , chemistry , isobaric process , tandem mass tag , proteome , proteomics , tandem mass spectrometry , reagent , scope (computer science) , computational biology , chromatography , tandem , quantitative proteomics , mass spectrometry , biochemistry , computer science , protein mass spectrometry , organic chemistry , physics , materials science , composite material , biology , gene , programming language , thermodynamics
Over the past decade, chemical labeling with isobaric tandem mass tags, such as isobaric tags for relative and absolute quantification reagents (iTRAQ) and tandem mass tag (TMT) reagents, has been employed in a wide range of different clinically orientated serum and plasma proteomics studies. In this review the scope of these works is presented with attention to the areas of research, methods employed and performance limitations. These applications have covered a wide range of diseases, disorders and infections, and have implemented a variety of different preparative and mass spectrometric approaches. In contrast to earlier works, which struggled to quantify more than a few hundred proteins, increasingly these studies have provided deeper insight into the plasma proteome extending the numbers of quantified proteins to over a thousand.