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Tandem affinity purification | TAP MS | Technique To Study Protein Protein Interactions |
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Tandem affinity purification (TAP) is an immunoprecipitation-based purification technique for studying protein–protein interactions.
The goal is to extract from a cell only the protein of interest, in complex with any other proteins it interacted with.
TAP uses two types of agarose beads that bind to the protein of interest
To enable the protein of interest to bind to the beads, it is tagged with a designed piece, the TAP tag.
The tandem-affinity-purification (TAP) tag consists of three component
two Immunoglobulin G (IgG) binding domains from the Staphylococcus aureus surface protein, Protein A and a calmodulin-binding peptide (CBP). These two parts are separated by a short peptide which is a target for the site-specific TEV protease: A widely-available protease originally isolated from Tobacco Etch Virus
The goal is to extract from a cell only the protein of interest, in complex with any other proteins it interacted with.
TAP uses two types of agarose beads that bind to the protein of interest
To enable the protein of interest to bind to the beads, it is tagged with a designed piece, the TAP tag.
The tandem-affinity-purification (TAP) tag consists of three component
two Immunoglobulin G (IgG) binding domains from the Staphylococcus aureus surface protein, Protein A and a calmodulin-binding peptide (CBP). These two parts are separated by a short peptide which is a target for the site-specific TEV protease: A widely-available protease originally isolated from Tobacco Etch Virus
Tandem affinity purification | TAP MS | Technique To Study Protein Protein Interactions |
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