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Quantitative proteomics using SILAC: Principles, applications, and developments
Author(s) -
Chen Xiulan,
Wei Shasha,
Ji Yanlong,
Guo Xiaojing,
Yang Fuquan
Publication year - 2015
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/pmic.201500108
Subject(s) - stable isotope labeling by amino acids in cell culture , quantitative proteomics , proteome , proteomics , computational biology , biology , biochemistry , gene
SILAC is based on direct addition of selected stable isotope amino acids into the cell culture medium, allowing superior quantitative analysis of the cellular proteome compared to other labeling methods. The great advantages of SILAC lie in its straight‐forward implementation, quantitative accuracy, and reproducibility over chemical labeling or label‐free quantification strategies, favoring its adoption for proteomic research. SILAC has been widely applied to characterize the proteomic changes between different biological samples, to investigate dynamic changes of protein PTMs, to distinguish specific interacting proteins in interaction proteomic analysis, and to analyze protein turnover in the proteome‐wide scale. The present review summarizes the principles of SILAC technology, its applications in biological research, and the present state of this technology.