Gel Filtration Chromatography - Find and share research.
Gel filtration, as known as size exclusion chromatography (SEC), separates proteins according to their different size as they pass through a gel filtration column. Compared to affinity chromatography or ion exchange chromatography, proteins to be seperated by gel filtration chromatography do not need to bind to the chromatography medium, making buffer composition hardly affect resolution.
Bio-Rad offers a useful Gel Filtration Standard. This calibration standard contains thyroglobulin (670 kD), to determine the void volume (Vo) of the column, as well as four additional proteins of 158, 44, 17, and 1.35 kD respectively.
Size-exclusion chromatography (also known as gel filtration chromatography) is a technique for separating proteins and other biological macromolecules on the basis of molecular size. Originally developed in the 1950s, the technique was developed using crosslinked dextran (1, 2).
Gel Filtration Chromatography Gel Filtration Chromatography The method mostly involves the separation of the proteins based on its molecular size. The proteins larger proteins are totally excluded from the gel and elute out first. The smaller proteins however, are small enough to move through the pores of the gel.
Desalting and buffer exchange use gel filtration chromatography to separate soluble macromolecules from smaller molecules. Desalting and buffer exchange are two of the most widely used gel filtration chromatography applications, and both can be performed using the same materials.
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Bio-Rad offers a selection of resins for separation by ion exchange, hydroxyapatite and fluoroapatite, affinity, size exclusion (gel filtration), and hydrophobic interaction chromatography. Get Help Call us at 1-800-4-BIORAD (1-800-424-6723).