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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...

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Related Experiment Video

Updated: Jun 16, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Published on: June 15, 2018

Bimolecular affinity purification (BAP): tandem affinity purification using two protein baits.

Gabriel N Maine1, Nathan Gluck, Iram W Zaidi

  • 1Department of Clinical Pathology, William Beaumont Hospital, Royal Oak, MI 48073, USA.

Cold Spring Harbor Protocols
|February 13, 2010
PubMed
Summary
This summary is machine-generated.

Tandem affinity purification (TAP) identifies protein complexes, but nonspecific interactions are a challenge. A new method, bimolecular affinity purification (BAP), uses two affinity tags on different proteins to improve specificity.

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Last Updated: Jun 16, 2026

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
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Identification of Protein Interacting Partners Using Tandem Affinity Purification
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Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Tandem affinity purification (TAP) is a method for protein complex characterization.
  • Nonspecific protein interactions can hinder the identification of true interacting partners.
  • TAP has been adapted for various organisms, including mammalian systems.

Purpose of the Study:

  • To describe a variation of TAP called bimolecular affinity purification (BAP).
  • To present a method for isolating or detecting molecular complex components.
  • To identify specific molecular complexes marked by two known components.

Main Methods:

  • Adaptation of the TAP procedure.
  • Placement of affinity moieties on two different proteins within a molecular complex.
  • Utilizing two sequential affinity purification steps.

Main Results:

  • Bimolecular affinity purification (BAP) offers improved specificity in identifying protein complexes.
  • The BAP method allows for the isolation and detection of specific molecular complexes.
  • This technique is suited for complexes with two known components.

Conclusions:

  • BAP is a valuable variation of TAP for specific molecular complex identification.
  • The method addresses challenges posed by nonspecific protein interactions.
  • BAP enhances the characterization of protein complexes in various biological systems.