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

Antibody Structure01:10

Antibody Structure

67.8K
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...
67.8K
Antibody Structure01:10

Antibody Structure

15.2K
15.2K
Hybridoma Technology01:31

Hybridoma Technology

18.6K
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,...
18.6K
Antibody Structure and Classes01:25

Antibody Structure and Classes

10.3K
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.
10.3K
Affinity and Avidity01:41

Affinity and Avidity

40.6K
Overview
40.6K
Antibody Actions01:26

Antibody Actions

3.9K
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...
3.9K

You might also read

Related Articles

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

Sort by
Same author

CD98hc-targeted antibody shuttles for central nervous system delivery with broad cross-species reactivity.

Nature biomedical engineering·2026
Same author

Ultra-Dilute Developability Analysis of Antibody Self-Association and Non-Specific Binding.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Machine learning predictions of IgG1 and IgG4 self-association and high-concentration solution properties.

mAbs·2026
Same author

Ginkgo Datapoints Antibody Developability Competition outcomes: limited model performance and a call for data standardization.

mAbs·2026
Same author

Bioconjugates for improved delivery of oligonucleotide therapeutics to the central nervous system.

Advanced drug delivery reviews·2026
Same author

Combining antibody conjugates with cytotoxic and immune-stimulating payloads maximizes anti-cancer activity.

Molecular oncology·2026

Related Experiment Video

Updated: Apr 5, 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

18.5K

Advances in Antibody Design.

Kathryn E Tiller1, Peter M Tessier1

  • 1Center for Biotechnology and Interdisciplinary Studies, Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180;

Annual Review of Biomedical Engineering
|August 15, 2015
PubMed
Summary

Optimizing therapeutic monoclonal antibodies involves enhancing attributes like binding and stability. Advances in antibody design methods are crucial for developing potent antibody therapeutics and overcoming current challenges.

Keywords:
CDRFabIgGVHcomplementarity-determining regionscFv

More Related Videos

Generation of Murine Monoclonal Antibodies by Hybridoma Technology
09:42

Generation of Murine Monoclonal Antibodies by Hybridoma Technology

Published on: January 2, 2017

44.2K
Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
12:55

Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries

Published on: January 17, 2015

19.4K

Related Experiment Videos

Last Updated: Apr 5, 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

18.5K
Generation of Murine Monoclonal Antibodies by Hybridoma Technology
09:42

Generation of Murine Monoclonal Antibodies by Hybridoma Technology

Published on: January 2, 2017

44.2K
Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
12:55

Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries

Published on: January 17, 2015

19.4K

Area of Science:

  • Biotechnology
  • Immunology
  • Pharmaceutical Sciences

Background:

  • Therapeutic monoclonal antibodies (mAbs) require optimization of critical attributes for efficacy.
  • Key attributes include binding affinity, specificity, stability, pharmacokinetics, and effector functions.
  • Compatibility with bispecific antibody formats and antibody-drug conjugates is also essential.

Purpose of the Study:

  • To review recent advancements in the design of monoclonal antibodies and fragments.
  • To highlight systematic design methods complementing traditional screening techniques.
  • To identify unmet challenges in antibody engineering for therapeutic applications.

Main Methods:

  • Review of literature on antibody design strategies.
  • Analysis of methods for optimizing binding loops, scaffolds, and domain interfaces.
  • Examination of approaches for modifying constant regions and bispecific architectures.

Main Results:

  • Significant progress has been made in designing antibody binding loops and scaffolds.
  • Systematic design methods offer powerful tools for enhancing antibody bioactivity.
  • New strategies for creating bispecific antibodies and antibody-drug conjugates have emerged.

Conclusions:

  • Antibody design is critical for developing effective therapeutics.
  • Further innovation in antibody engineering is needed to address remaining challenges.
  • Optimized antibody design promises more potent and versatile therapeutic options.