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Hybridoma Technology

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,...

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Updated: May 5, 2026

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

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

Murine V lambda x and V lambda x-containing antibodies bind human myelin basic protein

F S Galin¹, C C Maier, S R Zhou

¹Department of Physiology and Biophysics, University of Alabama at Birmingham 35294, USA.

The Journal of Clinical Investigation

|January 15, 1996

Summary

This summary is machine-generated.

Researchers found a unique link between V lambda x light chains and myelin basic protein (MBP) reactivity. This suggests a potential role for V lambda x in experimental allergic encephalomyelitis (EAE), an animal model of multiple sclerosis.

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

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

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

Published on: March 24, 2017

Area of Science:

Immunology
Neuroscience
Molecular Biology

Background:

Myelin basic protein (MBP) is a key autoantigen in experimental allergic encephalomyelitis (EAE), a model for multiple sclerosis.
The V lambda x light chain is rarely used in antibodies, and its antigen specificity is largely unknown.

Purpose of the Study:

To investigate if other antibodies with V lambda x light chains share antigen specificity with MBP.
To explore the role of the V lambda x light chain in antibody binding to MBP.

Main Methods:

Screening of V lambda x-containing monoclonal and polyclonal antibodies for reactivity with MBP.
Characterization of epitope specificity using MBP peptides.
Analysis of recombinant V lambda x binding to MBP.

Main Results:

All tested V lambda x-containing antibodies, unlike controls, bound MBP.
The V lambda x light chain significantly contributes to MBP binding.
Most V lambda x antibodies recognized an epitope within MBP residues 25-34, distinct from the F28C4 epitope (MBP Ac 1-9).

Conclusions:

A unique association exists between V lambda x expression and MBP reactivity.
The findings imply a potential role for V lambda x in the pathogenesis of EAE due to sequence homology with T cell receptors.