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Updated: May 4, 2026

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Profiling native kinases by immuno-assisted activity-based profiling.

Eric Okerberg¹, Ann Shih, Heidi Brown

¹ActivX Biosciences, La Jolla, California.

Current Protocols in Chemical Biology

|January 7, 2014

Summary

This summary is machine-generated.

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This study introduces novel methods using activity-based probes and western blotting to precisely measure small-molecule inhibitor interactions with kinases. These techniques enable quantitative analysis of inhibitor efficacy, selectivity, and protein binding in cells.

Area of Science:

Biochemistry
Molecular Biology
Chemical Biology

Background:

Kinases play crucial roles in cellular signaling pathways.
Dysregulation of kinase activity is implicated in numerous diseases, making them key therapeutic targets.
Understanding small-molecule inhibitor interactions with kinases is essential for drug development.

Purpose of the Study:

To develop efficient and cost-effective protocols for assessing small-molecule inhibitor interactions with native kinases.
To analyze kinase interactions with binding partners within a cellular context.
To quantitatively measure inhibitor efficacy, isoform selectivity, and post-translational modifications.

Main Methods:

Utilizing activity-based probes for specific labeling of kinase activity.

Keywords:

activity based protein profiling immuno-assisted activity based profiling inhibitors native kinases

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Last Updated: May 4, 2026

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Assaying Protein Kinase Activity with Radiolabeled ATP

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Published on: October 23, 2019

Employing western blotting procedures for quantitative analysis.

Integrating these methods to study protein-protein interactions.

Main Results:

Demonstrated efficient and cost-effective determination of small-molecule inhibitor-kinase interactions.
Enabled quantitative measurement of inhibitor efficacy and isoform selectivity.
Successfully identified noncovalent protein-protein interactions involving probe-labeled proteins.

Conclusions:

The described protocols offer a robust platform for kinase inhibitor research.
These methods facilitate comprehensive analysis of kinase behavior and drug interactions in cellular environments.
The approach aids in the discovery and characterization of novel kinase-targeted therapeutics.