Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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...
Antibody Actions01:26

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Cross-reactivity00:42

Cross-reactivity

Overview
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antigens Involved in Adaptive Immunity01:26

Antigens Involved in Adaptive Immunity

An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Inclusive Search for Anomalous Single-Photon Production in MicroBooNE.

Physical review letters·2026
Same author

First Search for Dark Sector e^{+}e^{-} Explanations of the MiniBooNE Anomaly at MicroBooNE.

Physical review letters·2026
Same author

Changes in personality functioning following psychotherapy: Utilizing machine learning to identify predictors in a psychodynamic psychotherapy sample.

Psychotherapy research : journal of the Society for Psychotherapy Research·2026
Same author

First Measurement of Charged-Current Muon-Neutrino-Induced K^{+} Production on Argon Using the MicroBooNE Detector.

Physical review letters·2026
Same author

Search for an Anomalous Production of Charged-Current ν_{e} Interactions without Visible Pions across Multiple Kinematic Observables in MicroBooNE.

Physical review letters·2025
Same author

First Measurement of ν_{e} and ν[over ¯]_{e} Charged-Current Single Charged-Pion Production Differential Cross Sections on Argon Using the MicroBooNE Detector.

Physical review letters·2025

Related Experiment Video

Updated: May 23, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

Modified C-reactive protein selectively binds to immunoglobulins.

M Boncler1, D Dudzińska, J Nowak

  • 1Department of Haemostasis and Haemostatic Disorders, Medical University of Lodz, Lodz, Poland. magdalena.boncler@umed.lodz.pl

Scandinavian Journal of Immunology
|April 11, 2012
PubMed
Summary

Modified C-reactive protein (mCRP) interactions with immunoglobulins are complex. Studies show mCRP binding to antibodies varies significantly, challenging the idea of a universal mCRP-immunoglobulin interaction.

More Related Videos

Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry
07:20

Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry

Published on: May 19, 2020

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
11:10

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Published on: June 29, 2016

Related Experiment Videos

Last Updated: May 23, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
07:26

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry
07:20

Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry

Published on: May 19, 2020

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
11:10

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study

Published on: June 29, 2016

Area of Science:

  • Immunology
  • Biochemistry
  • Protein interactions

Background:

  • Modified C-reactive protein (mCRP) is known to bind immunoglobulins non-specifically.
  • The precise nature and extent of these interactions remain unclear.
  • Understanding these interactions is crucial for interpreting mCRP's role in immune responses.

Purpose of the Study:

  • To investigate the binding of antibodies against human serum albumin (HSA) and IgG to mCRP and other plasma proteins.
  • To examine the binding of mCRP to antibodies targeting CRP signaling receptors (anti-CD32, anti-CD16).
  • To elucidate the specificities and characteristics of mCRP-immunoglobulin interactions.

Main Methods:

  • Enzyme-Linked Immunosorbent Assay (ELISA) was employed to quantify protein binding.
  • Western immunoblotting was utilized to analyze protein interactions.
  • Purified proteins including mCRP, fibrinogen (Fg), IgG, fibronectin (Fn), and C1q were tested.

Main Results:

  • Antibodies bound to contaminants within purified proteins and directly to some proteins like C1q, mCRP, and Fg.
  • Albumin presence and protein purity influenced anti-HSA binding effectiveness.
  • Binding of anti-HSA and anti-IgG to mCRP was lower than to plasma proteins, with variable direct interaction strengths.

Conclusions:

  • The binding of mCRP to immunoglobulins is not a universal phenomenon.
  • Specific antibody-protein interactions are influenced by various factors including protein purity and antibody specificity.
  • Further research is needed to fully characterize the complex binding dynamics between mCRP and immunoglobulins.