Related Experiment Video

Updated: Oct 12, 2026

Detection of True IgE-expressing Mouse B Lineage Cells
09:40

Detection of True IgE-expressing Mouse B Lineage Cells

Published on: December 1, 2014

Monoclonal antibodies against human IgE. Identification of an epitope sharing properties with the high-affinity

J Moscoso del Prado1, L Jimeno, T Obispo

  • 1Departamento de Investigación Biológica, Alergia e Inmunología Abelló S.A., Madrid, Spain.

Molecular Immunology
|August 1, 1991
PubMed

Three monoclonal antibodies to human IgE are described. One of them recognizes an epitope located within a region of 76 amino acids that has been shown to contain the Fc epsilon RI binding site. That epitope is shown to be susceptible to heating and to alkylation of cysteines involved in inter heavy chain bonds, but not to their reduction alone. In addition, this monoclonal antibody, although having a high affinity for free IgE, is unable to bind Fc epsilon RI-linked IgE. Based on these results, we discuss the possibility that the antibody recognizes the Fc epsilon RI binding site of the IgE molecule.

More Related Videos

Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study11:10

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

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

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...
Affinity and Avidity01:41

Affinity and Avidity

Overview
Cross-reactivity00:42

Cross-reactivity

Overview
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...
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 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.