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Updated: May 13, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

A universal and multiplex kinase assay using γ-[(18)O(4)]-ATP.

Chuan Fu¹, Xueyun Zheng, Yao Jiang

¹Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, PR China.

Chemical Communications (Cambridge, England)

|February 27, 2013

Summary

A novel non-radioactive method using γ-[(18)O4]-ATP enables multiplex kinase assays. This approach is broadly applicable, allowing for the assessment of inhibitor effectiveness and specificity across various kinases without specialized reagents.

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Area of Science:

Biochemistry
Enzymology
Chemical Biology

Background:

Kinase activity assays are crucial for drug discovery and biological research.
Current methods often rely on radioactive substrates or purified enzymes, limiting their scope and application.
Developing non-radioactive, versatile assay platforms is a significant need in the field.

Purpose of the Study:

To develop a novel, non-radioactive, and multiplex assay for kinase activity.
To demonstrate the broad applicability of this method across different kinases.
To enable the assessment of kinase inhibitor effectiveness and specificity.

Main Methods:

Synthesis of γ-[(18)O4]-adenosine triphosphate (ATP).
Development of a non-radioactive assay utilizing the synthesized ATP analog.

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Last Updated: May 13, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

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

Oligopeptide Competition Assay for Phosphorylation Site Determination

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Application of the assay to evaluate kinase activity and inhibitor profiles.

Main Results:

Successful synthesis of γ-[(18)O4]-ATP.
Establishment of a robust non-radioactive assay applicable to various kinases.
Demonstration of the method's utility in determining inhibitor effectiveness and specificity without purified enzymes or fluorescent substrates.

Conclusions:

The developed γ-[(18)O4]-ATP based method offers a versatile and non-radioactive approach for kinase research.
This novel assay platform simplifies kinase inhibitor screening and characterization.
The method's broad applicability and lack of requirement for specialized reagents make it a valuable tool for biochemical and pharmacological studies.