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Immunoprecipitation

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
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Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Updated: Jun 7, 2026

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

Solid-phase preparation of protein complexes.

Paolo Pengo¹, Gianluca Veggiani, Kwanchai Rattanamanee

¹Xeptagen SpA, Via delle Industrie 9, Marghera-Venezia I-30175, Italy. pengo@xeptagen.com

Journal of Molecular Recognition : JMR

|November 2, 2010

Summary

This summary is machine-generated.

This study introduces a continuous-flow, solid-phase method for protein complex assembly, reducing material needs and enabling solid-phase reuse. This novel approach preserves protein immunoreactivity for applications in immunometric analysis.

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The MultiBac Protein Complex Production Platform at the EMBL

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

Biochemistry
Chemical Engineering
Immunology

Background:

Traditional protein-protein conjugation methods require concentrated solutions and extensive purification.
Developing efficient and reusable methods for protein complex assembly is crucial for various applications.

Purpose of the Study:

To present a novel continuous-flow solid-phase approach for protein complex assembly.
To minimize material requirements and enable repeated use of the solid support.
To preserve the immunoreactivity of protein components for analytical applications.

Main Methods:

Utilized an immunoaffinity matrix as a solid support for reversible protein binding.
Employed the avidin-biotin system for mild and rapid tethering of protein components.
Developed a sequential immobilization and assembly process for protein complexes.
Implemented a pH-mediated release mechanism for recovering assembled complexes.

Main Results:

Successfully assembled protein complexes on a reusable solid phase with minimal material usage.
Demonstrated the preservation of immunoreactivity in the assembled protein complexes.
Prepared and validated immunoaffinity reagents mimicking native squamous cell carcinoma antigen-immunoglobulin M (SCCA-IgM) and alphafetoprotein-immunoglobulin M (AFP-IgM) immune complexes.
Confirmed the reusability of the solid phase without loss of binding capacity.

Conclusions:

The developed continuous-flow solid-phase method offers an efficient alternative to solution-phase protein conjugation.
This approach is versatile and applicable to the preparation of diverse protein assemblies.
The method is particularly suitable for generating high-quality immunoaffinity reagents for immunometric assays.