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Immunoprecipitation01:20

Immunoprecipitation

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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.
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Immunocytochemistry (ICC) and immunohistochemistry (IHC) are techniques that use antibodies to check for specific proteins or antigens in a sample. The technique was first published by Albert Coons in 1941 to detect the presence of pneumococcal antigen in tissue sections from mice infected with Pneumococcus. Immunocytochemistry helps localization of proteins or antigens in individual cells like blood cells, stem cells, etc., while immunohistochemistry does the same for tissue samples.
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Enzyme-Linked Immunosorbent Assay01:33

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In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
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Chromatin Immunoprecipitation- ChIP02:36

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Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
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Related Experiment Video

Updated: Sep 26, 2025

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
09:40

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

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Co-immunoprecipitation Assays.

Ian M Evans1, Ketevan Paliashvili2

  • 1Breast Cancer Research, Cancer Stem Cell Team, Institute of Cancer Research, Chester Beatty Laboratories, London, UK. ian.evans@icr.ac.uk.

Methods in Molecular Biology (Clifton, N.J.)
|April 22, 2022
PubMed
Summary
This summary is machine-generated.

Co-immunoprecipitation is a common method to identify protein interactions. This guide explains how to perform and analyze this technique, including its limitations.

Keywords:
Protein–protein interactionSignal transductionVEGFp130Cas

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Co-immunoprecipitation (Co-IP) is a widely used biochemical technique.
  • It is employed to identify protein-protein interactions within a biological complex.
  • The method relies on immunoprecipitation to isolate protein complexes.

Purpose of the Study:

  • To provide a comprehensive overview of the co-immunoprecipitation technique.
  • To offer a step-by-step guide for performing co-immunoprecipitation experiments.
  • To discuss the inherent limitations of co-immunoprecipitation.

Main Methods:

  • Utilizing antibodies to precipitate a target protein from a cell lysate.
  • Identifying co-precipitated proteins using techniques like Western blotting.
  • Analyzing the results to confirm protein interactions.

Main Results:

  • Co-immunoprecipitation successfully isolates protein complexes.
  • The technique can determine if two proteins interact in vivo.
  • Limitations include potential for false positives and negatives.

Conclusions:

  • Co-immunoprecipitation is a valuable tool for studying protein interactions.
  • Understanding the technique's principles and limitations is crucial for accurate results.
  • Further analysis is often required to validate protein interactions.