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Table 1 Overview of selected protein profiling technologies

From: Comparing protein abundance and mRNA expression levels on a genomic scale

Technology Type of labeling required Ability to detect many post-translational modifications Biomolecules that are optimally quantified Approximate dynamic range (and reference) Number of proteins/spots quantified (and reference)
Two-dimensional gel electrophoresis Silver staining Yes Naturally occurring forms of proteins larger than 10 kDa 10 [9] 1,500 [8]
Differential two-dimensional fluorescence gel electrophoresis (DIGE) In vitro with Cy2, Cy3 or CY5 fluorophores at primary amines Yes Naturally occurring forms of proteins larger than 10 kDa 10,000 [9] 1,100 [51]
SELDI- or MALDI-MS disease biomarker discovery None Yes Naturally occurring forms of proteins smaller than 10 kDa 25 Not applicable
Isotope-coded affinity tag (ICAT) - LC/MS In vitro with H1/D or C12/C13 ICAT reagent at cysteine No Cysteine-containing tryptic peptides from digests of protein extracts 10,000* 496 [18]
N14/N15 - LC/MS In vivo at nitrogens in amino acids Yes Tryptic peptides from digests of protein extracts 10,000 [19] 872 [20]
  1. *Assumed to be similar to that for multidimensional protein identification. Abbreviations: SELDI-MS, surface-enhanced laser desorption ionization mass spectrometry; MALDI-MS, matrix-assisted laser desorption ionization mass spectrometry; LC/MS, liquid chromatography and mass spectrometry.