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• W1554426397 abstract "Proteomics research involves the identification and characterisation of proteins in order to elucidate their function and interactions with other proteins. Since the composition of protein mixtures can vary between cell types and can change under certain physiological conditions, one aim is often to quantify upor down-regulation of individual proteins. Characterisation of proteomic changes associated with disease often helps to shed light on disease mechanisms and identify useful biomarkers and therapeutic targets. It is rarely the case that such proteins are either “present” or “absent”, but more likely that they vary in abundance to different degrees. It is therefore important to have a sensitive and accurate method to measure these changes using an unbiased approach. Shotgun proteomics approaches enable identification of proteins that are up-regulated or down-regulated under specific conditions and this can be studied in different cell and tissue lysates. Isobaric tags for relative and absolute quantification (iTRAQTM) make it possible to both identify and quantify proteins simultaneously. iTRAQTM can easily be multiplexed, enabling analysis of up to 8 different samples within the same experiment. Our objectives in this chapter are to place iTRAQTM (isobaric tags for relative and absolute quantification) in context in the history of attempts to bring quantitative studies to proteomics, to explain what it can do, to describe in some detail the protocol that we use in this laboratory and to illustrate the application of iTRAQTM to medical and clinically-relevant problems, including our own work on the proteomic effects of common drug treatments." @default.
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• W1554426397 date "2012-02-24" @default.
• W1554426397 modified "2023-09-25" @default.
• W1554426397 title "Quantitative Proteomics Using iTRAQ Labeling and Mass Spectrometry" @default.
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• W1554426397 doi "https://doi.org/10.5772/31469" @default.
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