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Related Experiment Videos

Stable isotope methods for high-precision proteomics.

Luke V Schneider1, Michael P Hall

  • 1Target Discovery Inc., 4015 Fabian Way, Palo Alto, CA 94303, USA. luke_schneider@targetdiscovery.com

Drug Discovery Today
|March 8, 2005
PubMed
Summary
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Stable isotope tagging coupled with mass spectrometry offers precise protein quantification and detects modifications missed by immunoassays. This approach enhances biomarker discovery and clinical diagnostics by eliminating sample bias and improving assay specificity.

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Stable isotope tagging enables precise relative protein quantification in mass spectrometry.
  • Mixing samples before processing eliminates recovery variations.
  • Mass spectrometry detects modifications missed by immunoassays, enhancing clinical relevance.

Purpose of the Study:

  • To review and compare stable isotope tagging methods for proteomics.
  • To evaluate these methods for biomarker discovery, target validation, and clinical diagnostics.

Main Methods:

  • Stable isotope labeling by amino acids in cell culture (SILAC)
  • Isotope-coded protein labeling (ICPL)
  • Dimethyl labeling
  • Isobaric tags for relative and absolute quantification (iTRAQ)

Related Experiment Videos

  • Tandem mass tags (TMT)

    • Main Results:

    • Stable isotope tagging offers high precision (CV < 10%) and eliminates sample-to-sample variation.
    • Mass spectrometry identifies post-translational modifications, splice variants, and mutations.
    • These methods overcome limitations of immunoassays like non-specific binding.

    Conclusions:

    • Stable isotope tagging methods are versatile tools in proteomics.
    • They are advantageous for biomarker discovery, validation, efficacy, toxicology screening, and diagnostics.
    • The choice of method depends on specific application requirements.