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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...

Chromatin Immunoprecipitation- ChIP

Chromatin Immunoprecipitation- ChIP

Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
Types of ChIP
ChIP can be divided into two types - X-ChIP and N-ChIP. X-ChIP involves in vivo cross-linking of histones and regulatory proteins to DNA, fragmenting the DNA by sonication, and isolating the protein-DNA...

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Related Experiment Video

Updated: Jun 19, 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

Automated Immunoprecipitation Workflow for Comprehensive Acetylome Analysis.

Marina A Gritsenko¹, Chia-Feng Tsai¹, Hyeyoon Kim¹

¹Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, USA.

Methods in Molecular Biology (Clifton, N.J.)

|July 25, 2024

Summary

This study introduces a fast, automated method for enriching lysine-acetylated peptides using magnetic beads. This magnetic bead-based immunoprecipitation improves reproducibility and comprehensiveness in acetylome analysis via mass spectrometry.

Keywords:

Acetyl peptide enrichment Acetylome Automation Immunoprecipitation Magnetic beads Mass spectrometry Post-translational modification Proteomics Lysine acetylation

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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

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Last Updated: Jun 19, 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

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Area of Science:

Biochemistry
Proteomics
Analytical Chemistry

Background:

Immunoprecipitation is crucial for enriching lysine-acetylated peptides for mass spectrometry-based acetylome analysis.
Current manual methods using agarose beads are time-consuming and prone to variability, leading to sample loss and reduced analytical sensitivity.
These limitations hinder comprehensive and robust acetylome profiling.

Purpose of the Study:

To develop a faster, automated protocol for lysine-acetylated peptide enrichment.
To improve the reproducibility and comprehensiveness of acetylome analysis.
To overcome the limitations of manual immunoprecipitation methods.

Main Methods:

Development of a magnetic bead-based immunoprecipitation reagent for automated peptide enrichment.
Application of the automated protocol for lysine-acetylated peptide isolation.
Analysis of enriched peptides using mass spectrometry for comprehensive acetylome profiling.

Main Results:

The automated protocol significantly reduces enrichment time compared to manual methods.
The magnetic bead-based approach enhances reproducibility and minimizes sample loss.
The method enables more comprehensive and robust acetylome analysis.

Conclusions:

The automated magnetic bead-based immunoprecipitation protocol offers a superior alternative to manual methods for acetylome analysis.
This advancement facilitates more efficient, sensitive, and reproducible large-scale studies of protein acetylation.
The protocol is suitable for comprehensive and robust acetylome profiling in various biological contexts.