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Related Concept Videos

Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as  cells...
Capillary Electrophoresis: Applications01:30

Capillary Electrophoresis: Applications

Capillary electrophoretic separations offer various modes, each with unique applications. These modes include capillary zone electrophoresis, capillary gel electrophoresis, capillary array electrophoresis, capillary isoelectric focusing, capillary isotachophoresis, micellar electrokinetic chromatography, and capillary electrochromatography.
Capillary zone electrophoresis (CZE) separates ionic components based on their electrophoretic mobility. It has been used to separate proteins, amino acids,...
Ion-Exchange Chromatography01:09

Ion-Exchange Chromatography

Ion-exchange chromatography, or IEC, is a technique for separating ions based on their affinity for the stationary phase. The stationary phase is a cross-linked polymer resin with covalently attached ionic functional groups. The functional groups can be either positively charged (cation exchangers) or negatively charged (anion exchangers). A cation exchanger consists of a polymeric anion and active cations, while an anion exchanger is a polymeric cation with active anions. The choice of...
Electrophoresis: Overview01:20

Electrophoresis: Overview

Electrophoresis is a powerful analytical separation technique that relies on the differential migration of charged species when subjected to an electric field. The core strength of electrophoresis lies in its ability to separate high-molecular-weight species in complex mixtures. It has found widespread use in biochemistry, molecular biology, and analytical chemistry, allowing the separation of compounds like amino acids, nucleotides, carbohydrates, and proteins with excellent resolution.
There...
Capillary Electrophoresis: Instrumentation01:20

Capillary Electrophoresis: Instrumentation

Capillary electrophoresis instrumentation typically consists of several key components. A high-voltage power supply generates the electric field necessary for the separation by connecting to an anode (the positively charged electrode) and a cathode (the negatively charged electrode) located in buffer reservoirs at each end of the capillary tube. The system includes a sample vial, a fused silica capillary tube coated with polyimide for mechanical strength through which the sample components...
Immunoprecipitation01:20

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: May 24, 2026

Ultra-High-Speed Western Blot using Immunoreaction Enhancing Technology
05:59

Ultra-High-Speed Western Blot using Immunoreaction Enhancing Technology

Published on: September 26, 2020

Crossed immunoelectrophoresis.

A Laine1

  • 1INSERM, Lille Cedex, France.

Methods in Molecular Biology (Clifton, N.J.)
|February 22, 2012
PubMed
Summary
This summary is machine-generated.

Crossed immunoelectrophoresis (CIE) offers superior protein separation and quantification compared to classical methods. This technique enhances resolution by combining two-dimensional electrophoresis with antibody-containing gels for precise analysis.

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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Related Experiment Videos

Last Updated: May 24, 2026

Ultra-High-Speed Western Blot using Immunoreaction Enhancing Technology
05:59

Ultra-High-Speed Western Blot using Immunoreaction Enhancing Technology

Published on: September 26, 2020

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Area of Science:

  • Immunology
  • Biochemistry
  • Analytical Chemistry

Background:

  • Crossed immunoelectrophoresis (CIE), also known as two-dimensional immunoelectrophoresis, was first described by Ressler in 1960.
  • Further refinements were made by Laurell, Clarke, Freeman, and Weeke.
  • CIE offers significant advantages over classical immunoelectrophoresis, including improved resolution and quantitative capabilities.

Purpose of the Study:

  • To detail the principles and methodology of crossed immunoelectrophoresis.
  • To highlight the advantages of CIE for protein analysis.
  • To explain the quantitative aspects of CIE.

Main Methods:

  • Combines electrophoretic separation of sample proteins in agarose gel.
  • Employs a second electrophoresis step perpendicular to the initial separation.
  • Utilizes an antibody-containing agarose gel for the second dimension.

Main Results:

  • Each separated protein forms a distinct precipitation peak.
  • The area under each peak is directly proportional to the protein concentration.
  • Peak area is inversely proportional to the antibody concentration in the antiserum.

Conclusions:

  • CIE provides enhanced resolution for complex protein mixtures.
  • The technique offers reliable quantitative analysis of specific proteins.
  • CIE is a powerful tool for protein profiling and characterization.