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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.
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Updated: Jan 19, 2026

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

Published on: February 6, 2018

Back-to-Germline (B2G) Procedure for Antibody Devolution.

Anja Schrade¹, Alexander Bujotzek¹, Christian Spick¹

¹Roche Pharma Research and Early Development (pRED), Large Molecule Research (LMR), Roche Innovation Center Munich, 82377 Penzberg, Germany.

Antibodies (Basel, Switzerland)

|September 24, 2019

Summary

This summary is machine-generated.

The back-to-germline (B2G) method generates antibody variants with tunable affinities, crucial for developing bispecific antibodies (bsAbs) with enhanced specificity for targeted cell therapies. This approach modulates antibody binding affinity without compromising specificity, offering a predictable alternative to current methods.

Keywords:

affinity antibody antigen binding maturation protein engineering structure

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Last Updated: Jan 19, 2026

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Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

Published on: September 14, 2018

Area of Science:

Immunology
Biotechnology
Protein Engineering

Background:

Bispecific antibodies (bsAbs) require binders with specific affinities for dual-antigen targeting.
Current methods for affinity modulation can be unpredictable or introduce unwanted properties.

Purpose of the Study:

To introduce a novel 'back-to-germline' (B2G) procedure for generating antibody derivatives with modulated affinities.
To create building blocks for avidity-enhanced bispecific antibodies with high specificity.

Main Methods:

Reversing B-cell maturation by introducing germline residues into antibody complementarity-determining regions (CDRs).
Focusing mutations on CDR residues with high antigen contact probability.
Generating VH, VL domains, and Fv combinations with varying degrees of 'de-maturation'.

Main Results:

The B2G procedure retains antibody specificity while modulating affinity, including creating extremely low-affinity binders detectable only in bivalent formats.
B2G demonstrated greater reliability and predictability compared to alanine replacement in CDRs.
The method successfully generated affinity-modulated monospecific variants for CD138, Her2/neu, and EGFR antibodies.

Conclusions:

The B2G procedure offers a reliable method for generating affinity-modulated antibodies for bsAb development.
This approach enables the creation of highly specific bsAbs by fine-tuning binding affinities.
B2G provides a predictable platform for antibody engineering without inducing poly-reactivity.