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Immunoprecipitation

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

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Related Experiment Video

Updated: Mar 2, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

Radioactive Pulse-Chase Analysis and Immunoprecipitation.

Javier G Magadán¹

¹Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.

|May 9, 2017

Summary

This study details a method for tracking influenza A virus (IAV) hemagglutinin (HA) protein synthesis and transport. Researchers use radioactive amino acids and specific biochemical techniques to analyze protein maturation and intracellular movement.

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Last Updated: Mar 2, 2026

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Area of Science:

Biochemistry
Molecular Biology
Virology

Background:

Quantitative analysis of protein fate is crucial for understanding cellular processes.
Radioactive amino acid labeling and immunoprecipitation are established biochemical techniques.
Studying influenza A virus (IAV) hemagglutinin (HA) transport is vital for understanding viral replication.

Purpose of the Study:

To describe a straightforward, step-by-step method for labeling newly synthesized IAV HA.
To enable quantitative analysis of HA maturation and transport through the secretory pathway.
To provide a protocol for researchers studying viral protein dynamics.

Main Methods:

Labeling newly synthesized proteins with radioactive amino acids ([³⁵S]-methionine).
Immunoprecipitation to isolate specific proteins (IAV HA).
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fluorography for detection and analysis.

Main Results:

Successful labeling of newly synthesized IAV HA with [³⁵S]-methionine.
Demonstration of the technique's ability to follow HA maturation and transport.
Validation of SDS-PAGE and fluorography for quantitative analysis of viral protein trafficking.

Conclusions:

The described method provides a simple and effective way to study IAV HA protein dynamics.
This technique facilitates the quantitative analysis of protein maturation and intracellular transport.
The protocol is valuable for research in virology and molecular cell biology.