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Related Concept Videos

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...
Chromatin Immunoprecipitation- ChIP02:36

Chromatin Immunoprecipitation- ChIP

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.
Types of ChIP
ChIP can be divided into two types - X-ChIP and N-ChIP. X-ChIP involves in vivo cross-linking of histones and regulatory proteins to DNA, fragmenting the DNA by sonication, and isolating the protein-DNA...

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Related Experiment Video

Updated: May 23, 2026

Immunoprecipitation with an Anti-Epitope Tag Affinity Gel to Study Protein-Protein Interactions
07:16

Immunoprecipitation with an Anti-Epitope Tag Affinity Gel to Study Protein-Protein Interactions

Published on: January 5, 2024

Immunoprecipitation: denaturing lysis.

Ed Harlow, David Lane

    CSH Protocols
    |April 10, 2012
    PubMed
    Summary
    This summary is machine-generated.

    Harsh lysis methods effectively release protein antigens for antibody-antigen complex formation and immunoprecipitation. However, this technique destroys noncovalent interactions and denaturation-sensitive epitopes, limiting its use in certain assays.

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    Last Updated: May 23, 2026

    Immunoprecipitation with an Anti-Epitope Tag Affinity Gel to Study Protein-Protein Interactions
    07:16

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    Published on: January 5, 2024

    Methylated DNA Immunoprecipitation
    21:24

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    Evaluation of Protein&#8211;Protein Interactions using an On-Membrane Digestion Technique
    07:07

    Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

    Published on: July 19, 2019

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Immunology

    Background:

    • Cell lysis is crucial for antigen extraction in immunological assays.
    • Traditional lysis methods may preserve or disrupt molecular interactions and epitopes.

    Purpose of the Study:

    • To describe a harsh lysis method for releasing protein antigens.
    • To evaluate the suitability of this method for subsequent antibody-antigen complex formation and immunoprecipitation.

    Main Methods:

    • Cells are treated with harsh, denaturing solutions to release protein antigens.
    • Lysates are diluted to reduce denaturing conditions for antibody-antigen complex formation.
    • Solutions are precleared prior to immunoprecipitation.

    Main Results:

    • This method efficiently releases most protein antigens.
    • Noncovalent protein-protein interactions are lost.
    • Denaturation-sensitive epitopes are destroyed.

    Conclusions:

    • Harsh lysis is suitable for antigen quantitation and identification of antibody-recognized polypeptide bands.
    • This method is appropriate for displaying denaturation-resistant epitopes.
    • It is not suitable for assays requiring intact noncovalent interactions or sensitive epitopes.