Mass Spec Service Organizations: Alternative solutions for SILAC™ sample processing
Protein Detection by Mass Spectrometry, John Leite, Invitrogen Corporation, Carlsbad, CA, USA
- Accounting for metabolic processes that affect in vivo labeling of cell culture using isotopic forms of amino acids in media
- Effect of shRNA knockdown of protein complex subunits on complex formation and quantitation using SILAC™ technique
Invitrosol™ Protein Solubilizers
- Enhanced sequence coverage of the peptide mass fingerprint for the nicotinic acetylcholine receptor
- Removal of monovalent cation adducts using a matrix additive during MALDI-TOF-MS analysis of peptides
- Multidimensional separation of membrane protein digests using immobilized pH gradients coupled to LC-MS for enhanced sequence coverage and confidence
Matthais Mann- University Southern Denmark, EMBO
- Ong, S.E. et al. Stable isotope labeling by amino acids in cell culture, SILAC™, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics. 1, 376-386 (2002).
Blagoev, B. et al. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 21, 315-318 (2003).
- Ong, S.E. et al. Properties of 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC™). J. Proteome Res. 2, 173-181 (2003).
- Ong, S.E. et al. Identifying and quantifying in vivo methylation sites by heavy methyl SILAC™. Nat. Methods. 1, 119-126 (2004).
Anderson, J.S. et al. Nucleolar proteome dynamics. Nature, 433, 77-83 (2005).
- Ibarrola, N. et al. A proteomic approach for quantitation of phosphorylation using stable isotope labeling in cell culture. Anal. Chem. 75, 6043-6049 (2003).
- Ibarrola, N. et al. A novel proteomic approach for specific identification of tyrosine kinase substrates using [13C]tyrosine. J. Biol. Chem. 279, 15805-15813 (2004).
- Amanchy, R. et al. Stable isotope labeling with amino acids in cell culture (SILAC™) for studying dynamics of protein abundance and posttranslational modifications. Sci. STKE. 267, pl2 (2005).
Xian Chen- Los Alamos National Laboratory
- Shui, W. et al. Enhancing TOF/TOF-based de novo sequencing capability for high throughput protein identification with amino acid-coded mass tagging. J. Proteome Res. 4, 83-90 (2005).
- Zhu, H. et al. Residue-specific mass signatures for the efficient detection of protein modifications by mass spectrometry. Anal. Chem. 74, 1687-1694 (2002).
- Chen, X. et al. Site-specific mass tagging with stable isotopes in proteins for accurate and efficient protein identification. Anal. Chem. 72, 1134-1143 (2000).
Steve Gygi- Harvard Medical School
- Everley, P.A. et al. Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research. Mol. Cell Proteomics. 3, 729-735 (2004).
- Gruhler, A. et al. Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling Pathway. Mol. Cell Proteomics. 4, 310-327 (2005).
Others: Al Burlingame (UCSF), Oda Yoshi (Inst of Seed Technology), Ruedi Aebersol (Institute for Molecular Systems Biology), Samir Hanash (Fred Hutchinson Cancer research center), Dr. Bernd Wollscheid (Institute for Systems Biology), Dan Fabris (University of Maryland Baltimore), Peter Ropestorff (University of Southern Denmark), Jan Schnitzer (Sidney Kimmel Cancer Center), plus many more
- Effect of shRNA knockdown of protein complex subunits on complex formation and quantitation using SILAC™ technique. Mahbod Hajivandi, John Leite, Xiquan Liang, Antje Taliana, Marieke Svoboda, Knut Maddden, Marshall R. Pope. 2005 American Society for Mass Spectrometry poster presentation.
- Quantification of membrane or membrane-bound proteins between normal and malignant cells isolated from the same patient with primary breast cancer. Xiquan Liang; Mahbod R. Hajivandi; Marshall Pope, 2005 American Society for Mass Spectrometry seminar presentation.