Premium
Use of antibodies for detection of phosphorylated proteins separated by two‐dimensional gel electrophoresis
Author(s) -
Kaufmann Hitto,
Bailey James E.,
Fussenegger Martin
Publication year - 2001
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200102)1:2<194::aid-prot194>3.0.co;2-k
Subject(s) - phosphorylation , proteome , dephosphorylation , gel electrophoresis , monoclonal antibody , protein phosphorylation , affinity electrophoresis , proteomics , biochemistry , biology , two dimensional gel electrophoresis , amino acid residue , antibody , microbiology and biotechnology , chemistry , computational biology , affinity chromatography , peptide sequence , protein kinase a , phosphatase , immunology , enzyme , gene
Protein phosphorylation and dephosphorylation are key regulatory mechanisms in prokaryotic and eukaryotic cells. Considering the role of phosphorylation in many human diseases, it appears a major challenge to refine on the methods to analyze the phospho‐proteome. Here we review the use of monoclonal antibodies directed against specific phosphorylated amino acid residues to visualize phosphoproteins separated by two‐dimensional gel electrophoresis. Strategies are described how this method can successfully be applied to create phospho‐proteome maps of mammalian cells.