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

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 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.

You might also read

Related Articles

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

Sort by
Same author

Examining the role of community health workers amid extreme weather events in low- and middle-income countries: a scoping review.

Public health·2024
Same author

EPIC: an evaluation of the psychological impact of early-phase clinical trials in cancer patients.

ESMO open·2022
Same author

Differential attainment, socioeconomic factors and surgical training.

Annals of the Royal College of Surgeons of England·2022
Same author

Perineal reconstruction supplemented by abdominal advancement following recurrent penile cancer: Two cases.

JPRAS open·2021
Same author

Orthognathic returns to theatre.

The British journal of oral & maxillofacial surgery·2021
Same author

A novel, low-cost digital nerve repair model.

Annals of the Royal College of Surgeons of England·2021

Related Experiment Video

Updated: Jun 3, 2026

Laboratory Scale Production and Purification of a Therapeutic Antibody
09:54

Laboratory Scale Production and Purification of a Therapeutic Antibody

Published on: January 24, 2017

Recent developments in antibody engineering.

M Little1, S Dübel, S Kipriyanov

  • 1Recombinant Antibody Group, German Cancer Research Center, Heidelberg, Germany.

Methods in Molecular Medicine
|March 11, 2011
PubMed
Summary
This summary is machine-generated.

Antibody engineering advanced by secreting functional antibody fragments from Escherichia coli. This enabled the creation and screening of bacterial antibody libraries for antigen binding.

More Related Videos

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction
11:02

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

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study
07:53

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study

Published on: August 16, 2019

Related Experiment Videos

Last Updated: Jun 3, 2026

Laboratory Scale Production and Purification of a Therapeutic Antibody
09:54

Laboratory Scale Production and Purification of a Therapeutic Antibody

Published on: January 24, 2017

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction
11:02

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

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study
07:53

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study

Published on: August 16, 2019

Area of Science:

  • Biotechnology
  • Molecular Biology
  • Immunology

Background:

  • Antibody engineering enables targeted therapies and diagnostics.
  • Secretion of functional antibody fragments from Escherichia coli (E. coli) was a key advancement.
  • Bacterial systems facilitate the production and screening of antibody libraries.

Purpose of the Study:

  • To detail the methods for generating and screening antibody libraries in E. coli.
  • To highlight the evolution of techniques for recombinant antibody production.

Main Methods:

  • Fusing bacterial signal peptides to antibody fragments for secretion from E. coli.
  • Utilizing polymerase chain reaction (PCR) to amplify immunoglobulin genes.
  • Screening bacterial supernatants using enzyme-linked immunosorbent assay (ELISA).
  • Employing bacteriophage lambda (λ) for efficient library transfection and screening.

Main Results:

  • Successful secretion of functional antibody fragments into E. coli periplasm and medium.
  • Establishment of E. coli-based antibody libraries for direct antigen screening.
  • Selection of immunogen-reactive recombinant antibodies via ELISA and radioactive screening.

Conclusions:

  • Bacterial systems provide a powerful platform for antibody discovery and engineering.
  • Technological improvements have enhanced the efficiency of antibody library screening.
  • Recombinant antibody technology has revolutionized the development of targeted biological agents.