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Related Experiment Video

Updated: May 12, 2026

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

Published on: January 12, 2024

Mass spectrometry based method to increase throughput for kinome analyses using ATP probes.

F E McAllister¹, M Niepel, W Haas

¹Department of Cell Biology, Harvard Medical School, Harvard University, Boston, Massachusetts 02115, United States.

Analytical Chemistry

|April 24, 2013

Summary

A new workflow using ActivX ATP probe (AAP) affinity reagents improves kinome-wide profiling throughput by 8-fold. This method enhances the analysis of kinase activity and abundance in various cell lines, aiding drug discovery.

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Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

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

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Published on: November 15, 2017

Area of Science:

Biochemistry
Proteomics
Cancer Biology

Background:

Protein kinases are crucial in biological processes and are key therapeutic targets.
Existing methods for kinome-wide profiling lack the throughput for comprehensive analysis.

Purpose of the Study:

To develop a high-throughput workflow for kinome-wide profiling.
To quantify relative kinase levels and modification states in cell lysates.

Main Methods:

Coupling ActivX ATP probe (AAP) affinity reagents with isotopic labeling.
Comparing the new workflow against a classical fractionation-based proteomics approach.
Utilizing phosphopeptide enrichment to analyze kinase activation states.

Main Results:

The AAP workflow enriched approximately 90 kinases in a single run, an 8-fold throughput increase.
AAPs effectively cross-linked both active and inactive kinase states.
Significant variations in kinase abundance, especially receptor tyrosine kinases, were observed across breast cancer subtypes.

Conclusions:

The improved kinome profiling method offers an effective means for systematic kinase analysis.
This approach aids in understanding cell signaling, oncogenic transformation, and drug effects.
Kinome profiling variations may explain differential drug sensitivities in breast cancer.