Proteomics
Proteomics
Mass spectrometry (MS)-based proteomics has become an essential tool for biologists over the last decade. The ability of a mass spectrometer to identify thousands of proteins from a complex biological sample has revolutionized scientific experiments. To fully understand the function of the proteome in health and disease, however, one must have the ability to accurately quantify proteins in many different types of biological samples.
The invention of faster and higher resolution mass spectrometers has enabled the quantification of complex proteome dynamics. Heavy stable isotopes are routinely employed to generate precise and accurate quantitative proteomic data. Peptides labelled with heavy stable isotopes share identical biochemical characteristics to “light” or unlabelled peptides except for a difference in mass. Mixing heavy peptides with light peptides results in peptide pairs that co-elute into the mass spectrometer, which can easily distinguish between the peptides based on the mass difference.
Quantifying differences between proteomes subjected to different biological conditions or experiments can be achieved when using the heavy peptides as an internal standard or a control. Cambridge Isotope Laboratories, Inc. offers a variety of stable isotope reagents for labelling any proteome for quantitative MS analysis. These stable isotope MS methods are bringing scientists closer to curing human diseases through quantitative biomarker analysis and quantitative proteomic analysis of animal models of disease.
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One type of proteome labelling introduces a stable isotope amino acid(s) to cell growth media or rodent feed. Growth and feeding periods allow the stable isotope-labelled amino acid(s) to become metabolically incorporated into the proteome.
To help expedite quality control (QC) and quantitation in proteomics, CIL offers a number of off-the-shelf kits. In general, the QC kits are designed to evaluate the performance of the LC-MS platform, either alone or in combination with the analytical workflow.
The incorporation of two 18O atoms into each C-terminus of peptides derived from proteolytic digestion of biological samples has emerged as one of the leading global labelling strategies used in comparative quantitative proteomics.
Isotopically labelled standards for proteomic measurements can be prepared chemically. This can be achieved at the peptide or protein level by solid phase synthesis or recombinant gene expression, respectively.
Chemical tagging refers to labelling proteins or peptides in vitro. This inexpensive method is advantageous over metabolic labelling due to its ability to label human samples and its low cost. In addition, chemical tagging can quantify more than two samples in one MS experiment.
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