Related Experiment Video

Updated: Oct 17, 2026

Proteomic Profiling of Macrophages by 2D Electrophoresis
07:53

Proteomic Profiling of Macrophages by 2D Electrophoresis

Published on: November 4, 2014

Solubilization of delipidated macrophage membrane proteins for analysis by two-dimensional electrophoresis

A Simões-Barbosa1, J M Santana, A R Teixeira

  • 1Department of Pathology, University of Brasília, Brazil.

Electrophoresis
|March 22, 2000
PubMed

More Related Videos

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry10:59

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Published on: May 21, 2018

Proteomic Analysis of Human Macrophage Polarization Under a Low Oxygen Environment10:15

Proteomic Analysis of Human Macrophage Polarization Under a Low Oxygen Environment

Published on: January 7, 2019

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...
SDS-PAGE01:27

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...