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Related Experiment Video

Updated: May 27, 2026

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
06:09

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

Optimized conditions for a quantitative SELDI TOF MS protein assay.

Lee Lomas1, Charlotte H Clarke, Vanitha Thulasiraman

  • 1Laboratory Separations Division, Bio-Rad Laboratories, Hercules, CA, USA. lee_lomas@bio-rad.com

Methods in Molecular Biology (Clifton, N.J.)
|November 16, 2011
PubMed
Summary

This study introduces a novel method for reproducible peptide and protein diagnostic assays using surface-enhanced laser desorption/ionization (SELDI) mass spectrometry. By incorporating a complex protein matrix, the assay achieves high quantitative reproducibility with less than 10% coefficient of variation.

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Related Experiment Videos

Last Updated: May 27, 2026

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
06:09

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification
09:04

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Biotechnology

Background:

  • Diagnostic test development relies on factors like sample availability and quantitative reproducibility.
  • Laser Desorption/Ionization Mass Spectrometry (LDI-MS) is suitable for peptide and protein analysis.
  • Surface-Enhanced Laser Desorption/Ionization (SELDI)-biochips enhance reproducibility and relative quantitation in MS.

Purpose of the Study:

  • To develop reproducible SELDI-based assays for peptide and protein diagnostics.
  • To establish a method for improved quantitative reproducibility in SELDI assays.
  • To present a strategy for internal normalization and reproducible ionization background.

Main Methods:

  • Incorporating a complex artificial protein matrix into the sample for analysis.
  • Utilizing the protein matrix to create a common and reproducible ionization background.
  • Employing internal normalization standards within the SELDI-MS assay.

Main Results:

  • Achieved quantitative assays with coefficients of variation (CVs) typically less than 10% across assays and days.
  • Demonstrated the successful implementation of the method using an E. coli protein matrix.
  • Outlined criteria for selecting suitable complex protein matrices for SELDI assay development.

Conclusions:

  • The developed SELDI assay method significantly enhances quantitative reproducibility.
  • The incorporation of a complex protein matrix is key to achieving reliable diagnostic assays.
  • The method is adaptable to various protein matrix sources provided specific criteria are met.