IsoTaG Biotin Azide Pack (CCT-1501)

Description

IsoTaG Biotin Azide probes take advantage of the mass shift of stable heavy isotope labels (SHLs) to enable mass-independent chemical proteomics platform that helps to address unique challenges of the proteome characterization. In this approach a unique isotopic signature is embedded exclusively into the peptides and it serves as a computationally recognizable full-scan MS reporter. A computational algorithm, termed isotopic signature transfer and mass pattern prediction (IsoStamp), for the detection of recoded species in full-scan mass spectra, was also developed by the Carolyn Bertozzi group. IsoTaG H/L Biotin Azide pack contains 2 mg of light [M] and heave [M+2] probe encoded by 2 C12 or 2 C13 atoms.

Specifications

Documents

Selected References

1. Woo, C.M., et al. (2015). Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis.Nat Methods., 12: 561-7. [PubMed]
2. Woo, C.M., et al. (2017). Development of IsoTaG, a Chemical Glycoproteomics Technique for Profiling Intact N- and O‑Glycopeptides from Whole Cell Proteomess. J. Proteome Res., 16: 1706−18. [PubMed]
3. Goa, G., et al. (2017). Small Molecule Interactome Mapping by Photoaffinity Labeling Reveals Binding Site Hotspots for the NSAIDs. J. Am. Chem. Soc., 140: 4259−68. [PubMed]
4. Weerapana, E., et al. (2010). Quantitative reactivity profiling predicts functional cysteines in proteomes. Nature 468: 790−5. [PubMed]
5. Woo, C.M., et al. (2017). Mapping and Quantification of Over 2000 O-linked Glycopeptides in Activated Human T Cells with Isotope-Targeted Glycoproteomics (Isotag). Mol. Cell. Proteomics 17: 764-75. [PubMed]