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Related Experiment Videos

Shotgun proteomics using the iTRAQ isobaric tags.

Kunal Aggarwal1, Leila H Choe, Kelvin H Lee

  • 1School of Chemical and Biomolecular Engineering, Cornell University, 120 Olin Hall, Ithaca, NY 14853-5201, USA. KHL9@cornell.edu.

Briefings in Functional Genomics & Proteomics
|June 15, 2006
PubMed
Summary

Isobaric tagging with iTRAQ reagents enables high-throughput proteome analysis. This review covers iTRAQ applications, compares it to other shotgun proteomic techniques, and discusses challenges in mass spectrometry-based protein identification.

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Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Shotgun proteomic methods are crucial for high-throughput proteomic analysis.
  • Isobaric tagging reagents, such as iTRAQ, facilitate simultaneous protein identification and quantitation across multiple samples using tandem mass spectrometry (MS).

Purpose of the Study:

  • To describe proteome analysis utilizing iTRAQ reagents.
  • To review current applications of iTRAQ reagents in proteomic studies.
  • To compare iTRAQ with other shotgun proteomic techniques regarding protein identification metrics.

Main Methods:

  • Utilizes isobaric tagging of peptides with iTRAQ reagents.
  • Employs tandem mass spectrometry (MS) for protein identification and quantitation.
  • Compares protein sequence and proteome coverage across different shotgun proteomic techniques.

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Main Results:

  • iTRAQ reagents enable simultaneous identification and quantitation of proteins in up to four samples.
  • Comparison of iTRAQ with other methods highlights differences in protein sequence and proteome coverage.
  • Discussion includes the importance of isotope purity correction for accurate protein quantitation.

Conclusions:

  • iTRAQ reagents are a valuable tool for high-throughput proteomic analysis.
  • Challenges remain in mass spectrometry-based proteomic analysis that impact protein identification depth.
  • Further advancements are needed to overcome limitations in current shotgun proteomic methods.