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In order to assess the biological function of proteins and their modifications for
understanding signaling mechanisms within cells as well as specific
biomarkers to disease, it is important to study the change of proteome under
different experimental conditions. The emerging technology of mass
spectrometry-based quantitative proteomics provides a powerful tool to
quantitatively and systematically assess quantitative differences in protein
profiles of distinct samples and is increasingly becoming a significant
component of biomedical and clinical research.
SILAC: stable isotope labeling of amino acids in cell culture,a global method
whereby all translated proteins have isotope labels metabolically incorporated
at selected amino acid residues;
ICAT: isotope-coded affinity tags, a technique that labels cysteine residues at
the protein level
iTRAQ: multiplexed isobaric tags for relative and absolute quantification;
GIST: global internal standard technology, a global post-digestion labeling
method that labels primary amine groups (peptide N-terminus and lysine
residues)
ISIL: an extension of GIST called in-gel stable isotope labeling, a method that
labels primary amine groups of proteins (protein N-terminus and lysine
residues) directly from gel separated samples.
Label-free: approaches to quantitative proteomics have gained prominence in
recent years since no additional chemistry or sample preparation steps are
required.
Mass spectrometry-based approaches for targeted protein quantification are
based on the concept of isotope dilution mass spectrometry techniques
commonly used for the detection of small molecules. The approach is
comparable to modern advanced antibody-based methods, such as the
multianalyte profiling platform (MAP), offering multiplexing detection capability
with an excellent dynamic range.