SILAC RPMI 1640, w/o L-Arginine, w/o L-Lysine, w/o L-Glutamine, w/o Phenol Red
SILAC RPMI 1640, w/o L-Arginine, w/o L-Lysine, w/o L-Glutamine, w/o Phenol Red is optimized for labeling experiments involving the use of stable amino acid isotopes (SILAC = stable isotope labeling with amino acids in cell culture). SILAC enables a simple, robust, and powerful approach in mass spectrometry (MS)-based quantitative research to explore the enormous complexity of the proteome. It is used to investigate various aspects, such as protein expression, protein quantification, and protein stability, which are difficult to detect with simple mass spectrometry.
SILAC labeling is accomplished via normal metabolic processes (e.g., cell division), by incorporating non-radioactive stable amino acid isotopes into newly synthesized proteins. In this process, the "light" amino acids contained in the growth medium are replaced by "heavy" ones. Cells growing in this medium take up the heavy amino acids and enable the differentiation between light and heavy proteins. These labeled target proteins can also be used for protein quantification. Protein levels are measured with a mass spectrometer, based on signal intensity (labeled cells appear heavier). By providing accuracy of quantification and the simplicity of interpreting MS results, the SILAC method offers unique advantages for quantitative and functional proteomics.
SILAC RPMI is formulated without L-arginine and L-lysine for multiple isotopic amino acid labeling and has no effect on cell morphology or growth rates.
- Quantitative and functional proteomics
- Analyses of tissue regeneration
- Analyses of post-translational modifications
- MS (Mass Spectrometry)
- NMR (Nuclear Magnetic Resonance)