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Related Concept Videos

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...
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...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Hybridoma Technology01:31

Hybridoma Technology

Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
Hybridoma Selection
Commonly used fusion techniques — electroporation, polyethylene glycol...
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...
Affinity and Avidity01:41

Affinity and Avidity

Overview

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Related Experiment Video

Updated: Jun 13, 2026

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions
07:35

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions

Published on: July 10, 2021

A novel heterophilic antibody interaction involves IgG4.

T Ito1, K Kitahara, T Umemura

  • 1Department of Medicine, Gastroenterology, Shinshu University School of Medicine, Matsumoto, Japan.

Scandinavian Journal of Immunology
|April 14, 2010
PubMed
Summary

Immunoglobulin G4 (IgG4) exhibits novel Fc-Fc interactions, distinct from classical rheumatoid factor (RF). This unique IgG4 binding to animal IgGs has diagnostic potential and explains assay interferences.

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Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
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Published on: February 23, 2018

Area of Science:

  • Immunology
  • Biochemistry

Background:

  • Immunoglobulin G4 (IgG4) is linked to various pathologies like autoimmune pancreatitis and idiopathic membranous nephropathy.
  • IgG4 possesses unique characteristics, including absent classical complement pathway activation and Fab-arm exchange.
  • Previous research identified IgG4's rheumatoid factor (RF)-like activity via Fc-Fc interaction, termed novel RF (NRF), contrasting with classical RF (CRF)'s Fab-Fc interaction.

Purpose of the Study:

  • To investigate heterophilic interactions of human IgG4 with animal immunoglobulins.
  • To compare the binding mechanisms of novel RF (NRF) with classical RF (CRF).
  • To explore the diagnostic implications and potential interferences related to IgG4's heterophilic binding.

Main Methods:

  • Testing human IgG4 reactivity against various animal IgGs.
  • Characterizing the binding site (Fab vs. Fc) of IgG4 to rabbit IgG.
  • Correlating IgG4 binding with its concentration in biological samples.

Main Results:

  • Human IgG4 demonstrated variable heterophilic reactivity, strongly binding to rabbit and mouse IgGs.
  • IgG4 binding to rabbit IgG was mediated by the Fc region, not the Fab region, consistent with NRF.
  • The observed binding correlated with IgG4 concentration, suggesting potential diagnostic utility and explaining assay interferences.

Conclusions:

  • A novel heterophilic antibody interaction involving IgG4 has been defined.
  • The universality of IgG4's unique Fc-Fc binding mechanism is established.
  • This Fc-Fc interaction has implications for understanding IgG4-related diseases and improving biological assay accuracy.