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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: Sep 24, 2025

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Published on: January 18, 2020

A Novel Method for Total IgE Purification from Human Serum.

Fariza Mishaal Saiema Badloe^1,2, Shauni De Vriese^1,3, Tina De Bruyn Carlier¹

¹Vrije Universiteit Brussel (VUB), SKIN Research Group, Brussels, Laarbeeklaan 103, 1090 Belgium.

Journal of Immunology (Baltimore, Md. : 1950)

|May 6, 2022

Summary

Researchers developed a new, accessible method to purify immunoglobulin E (IgE) from human serum. This technique yields high-purity IgE, crucial for advancing allergy research and in vitro/in vivo models.

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Last Updated: Sep 24, 2025

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Published on: January 18, 2020

IgY Technology: Extraction of Chicken Antibodies from Egg Yolk by Polyethylene Glycol PEG Precipitation

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Published on: May 1, 2011

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

Published on: July 27, 2016

Area of Science:

Immunology
Biochemistry
Allergy Research

Background:

High-affinity chromatography is standard for antibody purification but requires specialized expertise and equipment.
Commercial kits for immunoglobulin E (IgE) purification are currently unavailable.
There is a need for accessible methods to purify human serum IgE for research.

Purpose of the Study:

To establish a novel and widely accessible method for purifying total IgE from human serum.
To ensure the purity and functionality of the purified IgE for experimental use.
To facilitate the use of IgE in allergy research models.

Main Methods:

Depletion of polyclonal IgG from human serum.
Capture and elution of total IgE using anti-human IgE antibody-coupled beads.
Incubation with protein G-coupled beads to enhance purity.
Analysis of purity and concentration using Western blot and ELISA.
Functional assessment of purified IgE using human mast cells.

Main Results:

The novel method effectively purified total IgE from human serum.
Purified IgE fractions demonstrated high purity with minimal IgG contamination.
Concentrations of purified IgE correlated with total serum IgE levels.
Purified IgE was functional, inducing mast cell degranulation (CD63+ expression and histamine release).

Conclusions:

A novel, effective, and accessible method for human serum IgE purification was established.
This method yields high-purity, functional IgE suitable for research applications.
The technique has the potential to improve IgE-based in vitro and in vivo models in allergy research.