Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)-Based Quantitative Proteomics and Phosphoproteomics in Fission Yeast | Zendy

Alejandro Carpy | Zendy; André Koch | Zendy; Claudia C. Bicho | Zendy; Weronika E. Borek | Zendy; Silke Hauf | Zendy; Kenneth E. Sawin | Zendy; Boris Maček | Zendy

Open Access

Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)-Based Quantitative Proteomics and Phosphoproteomics in Fission Yeast

Author(s) -

Alejandro Carpy,

André Koch,

Claudia C. Bicho,

Weronika E. Borek,

Silke Hauf,

Kenneth E. Sawin,

Boris Maček

Publication year - 2017

Publication title -

cold spring harbor protocols

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.674

H-Index - 51

eISSN - 1940-3402

pISSN - 1559-6095

DOI - 10.1101/pdb.prot091686

Subject(s) - stable isotope labeling by amino acids in cell culture , phosphoproteomics , phosphopeptide , proteome , chemistry , mass spectrometry , proteomics , isobaric labeling , quantitative proteomics , orbitrap , chromatography , amino acid , biochemistry , computational biology , protein phosphorylation , phosphorylation , biology , protein kinase a , gene

Modern mass spectrometry (MS)-based approaches are capable of identifying and quantifying thousands of proteins and phosphorylation events in a single biological experiment. Here we present a (phospho)proteomic workflow based on in-solution proteome digestion of samples labeled by stable isotope labeling by amino acids in cell culture (SILAC) and phosphopeptide enrichment using strong cation exchange (SCX) and TiO chromatographies. These procedures are followed by high-accuracy MS measurement on an Orbitrap mass spectrometer and subsequent bioinformatic processing using MaxQuant software.

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