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Related Experiment Video

Updated: Sep 3, 2025

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

Filter trapping protocol to detect aggregated proteins in human cell lines.

Jagat K Chhipi-Shrestha¹, Minoru Yoshida², Shintaro Iwasaki³

¹Chemical Genomics Research Group, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.

|July 26, 2022

Summary

Researchers developed an improved filter-trapping assay to detect aggregated proteins in human cells. This method aids in understanding aging and neurological diseases by identifying cytotoxic protein aggregates.

Keywords:

Molecular Biology Protein Biochemistry Protein expression and purification

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Last Updated: Sep 3, 2025

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Label-Free Immunoprecipitation Mass Spectrometry Workflow for Large-scale Nuclear Interactome Profiling

Published on: November 17, 2019

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

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Published on: December 9, 2016

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

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Published on: May 22, 2020

Area of Science:

Biochemistry
Cell Biology
Neuroscience

Background:

Loss of protein homeostasis leads to cytotoxic protein aggregates.
Protein aggregates are a hallmark of aging and neurological diseases.

Purpose of the Study:

To present an adjusted filter-trapping assay protocol for detecting global aggregated proteins in human cell lines.
To provide an alternative method for monitoring specific protein aggregates using immunoblotting.

Main Methods:

Utilized an adjusted filter-trapping assay.
Employed a high-sensitive protein staining method.
Incorporated immunoblotting for specific protein aggregate detection.

Main Results:

Successfully detected global aggregated proteins in human cell lines.
Demonstrated the capability to monitor specific protein aggregates, both ectopically expressed and endogenous.

Conclusions:

The developed assay is a valuable tool for studying protein aggregation in the context of aging and neurological disorders.
This protocol facilitates the investigation of cytotoxic protein aggregates, contributing to a better understanding of disease mechanisms.