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Related Concept Videos

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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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...
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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...
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Related Experiment Video

Updated: Jun 16, 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

Commonly used tag combinations for tandem affinity purification.

Yifeng Li1

  • 1Department of Anesthesiology, David Geffen School of Medicine, 650 Charles E. Young Drive, University of California, Los Angeles, Los Angeles, CA 90095, USA. wu0915@ucla.edu

Biotechnology and Applied Biochemistry
|February 17, 2010
PubMed
Summary
This summary is machine-generated.

Tandem affinity purification (TAP) isolates proteins and their partners. This review covers various TAP tag combinations for improved yields and unique features in protein complex identification.

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Last Updated: Jun 16, 2026

Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
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10:36

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

Published on: July 27, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Tandem affinity purification (TAP) is crucial for isolating protein complexes.
  • The method, initially for yeast, is now widely used across organisms.
  • TAP combined with mass spectrometry (MS) is vital for systematic protein complex identification.

Purpose of the Study:

  • To review various tandem affinity purification (TAP) tag combinations.
  • To highlight alternative TAP tags with improved yields or unique features.
  • To guide the selection and development of TAP tags for specific research applications.

Main Methods:

  • Overview of different dual-affinity tag combinations for TAP.
  • Discussion of alternative affinity handles used in TAP tags.
  • Analysis of TAP tag performance in protein complex isolation.

Main Results:

  • The review details diverse TAP tag designs.
  • Alternative tags offer enhanced protein complex isolation efficiency.
  • Specific tag combinations provide unique advantages for different applications.

Conclusions:

  • TAP is an essential technique for proteomic studies.
  • The choice of TAP tag significantly impacts experimental outcomes.
  • Further development of TAP tags will advance protein complex research.