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Related Concept Videos

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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...
Affinity Chromatography01:03

Affinity Chromatography

Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

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Related Experiment Video

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Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
11:30

Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells

Published on: January 26, 2017

The tandem affinity purification method: an efficient system for protein complex purification and protein interaction

Xiaoli Xu1, Yuan Song, Yuhua Li

  • 1Key Laboratory of Arid and Grassland Agroecology of Ministry of Education, School of Life Sciences, Lanzhou University, Lanzhou 730000, China.

Protein Expression and Purification
|April 20, 2010
PubMed
Summary

The tandem affinity purification (TAP) method enables protein complex analysis across various organisms. This review details TAP method modifications, applications, and future prospects for identifying protein interactions.

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Last Updated: Jun 13, 2026

Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
11:30

Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells

Published on: January 26, 2017

Identification of Protein Interacting Partners Using Tandem Affinity Purification
10:02

Identification of Protein Interacting Partners Using Tandem Affinity Purification

Published on: February 25, 2012

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
08:23

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Proteomics

Background:

  • Understanding protein interactions is crucial for elucidating cellular functions and molecular mechanisms.
  • The tandem affinity purification (TAP) method was initially developed for yeast to purify protein complexes and identify protein-protein interactions.

Purpose of the Study:

  • To review the applications of the TAP method in diverse organisms.
  • To discuss modifications and advancements in TAP tag technology.
  • To explore the limitations and future potential of TAP for protein complex analysis.

Main Methods:

  • Literature review of the TAP method and its variations.
  • Analysis of TAP method applications across different biological systems (yeast, mammalian, plant, bacteria).
  • Examination of tag modifications and their impact on purification efficiency.

Main Results:

  • The TAP method has been successfully adapted for protein complex analysis in various organisms beyond yeast.
  • Numerous modifications to the original TAP tag have enhanced its applicability and efficiency.
  • The review covers disadvantages, recent developments, and future directions for the TAP technique.

Conclusions:

  • The TAP method is a versatile and adaptable technique for protein complex purification and interaction studies.
  • Ongoing modifications and developments continue to expand the utility of TAP in biological research.
  • The future prospects of TAP involve further refinement for high-throughput analysis and complex interactome mapping.