title: Proteomic analysis of pluripotent stem cells.
abstract: Mass spectrometry (MS)-based proteomics has become one of the most powerful tools for identifying expressed proteins, providing quick insights into molecular and cellular biology. Traditionally, proteins isolated by either one- or two-dimensional gel electrophoresis are digested with a site specific protease. The resulting peptides are subject to one of two forms of analysis: (1) matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) MS, where a "mass fingerprint" of all the peptides in a sample is generated, or (2) electrospray ionization tandem MS (ESI-MS/MS), where a mass fragmentation spectra is generated for each peptide in a sample. The resulting mass information is then compared to that of a theoretical database created with available genomic sequence information. This unit provides protocols for this type of assessment in embryonic stem cells (ESCs).
authors.affiliation: University of Western Ontario, London, Ontario, Canada.
authors.forename: Sean C
authors.initials: SC
authors.lastname: Bendall
authors.forename: Aaron T
authors.initials: AT
authors.lastname: Booy
authors.forename: Gilles
authors.initials: G
authors.lastname: Lajoie
mesh_terms: D006801:Humans; D039904:Pluripotent Stem Cells / Q000378:metabolism*; D011506:Proteins / Q000235:genetics / Q000302:isolation & purification; D040901:Proteomics / Q000379:methods*; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D011506:Proteins