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

15.3K
15.3K
Antibody Structure01:10

Antibody Structure

69.4K
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...
69.4K
Immunoprecipitation01:20

Immunoprecipitation

8.1K
Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
8.1K
Cross-reactivity00:42

Cross-reactivity

34.0K
Overview
34.0K
Antibody Structure and Classes01:25

Antibody Structure and Classes

10.5K
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.
10.5K
Hybridoma Technology01:31

Hybridoma Technology

18.7K
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,...
18.7K

You might also read

Related Articles

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

Sort by
Same author

A machine learning approach to identify active polysorbate 20 degrading hydrolases in biopharmaceutical formulations.

Journal of pharmaceutical sciences·2026
Same author

Discovery of a chimeric transposase-transposon system for advanced genome engineering.

iScience·2026
Same author

Glycan pairing in therapeutic IgG orchestrates Fcγ receptor engagement and ADCC: an integrated structure-function approach for thorough evaluation of Fc N-glycans as critical quality attributes.

mAbs·2026
Same author

Phosphatidylcholine-Polysorbate 20-Based Mixed Micelles: A New Option to Prevent Protein Aggregation?

Pharmaceutics·2026
Same author

Selective clearance of monoclonal antibodies via the mannose receptor is dependent on glycan pairing.

Scientific reports·2026
Same author

Safety, tolerability, pharmacokinetics and pharmacodynamics of the spleen tyrosine kinase inhibitor BI 894416 in healthy volunteers and patients with asthma.

British journal of pharmacology·2026
Same journal

Discovery and optimization of a pH-responsive ultra-long-acting VHH-based growth hormone mimetic.

mAbs·2026
Same journal

Efficient inference of non-polyreactive antibody variants dependent on local fine-tuning.

mAbs·2026
Same journal

Impact of ASO conjugation and receptor binding affinity on intracellular transport of mono- and bispecific TfR- and CD98-Brainshuttle<sup>TM</sup> variants.

mAbs·2026
Same journal

Development of single-chain C1q affinity chromatography-mass spectrometry for the glycoform-resolved characterization of low-affinity immunoglobulin G interactions.

mAbs·2026
Same journal

Biparatopic targeting of IL-23 enables dual-epitope engagement and enhanced neutralization potency.

mAbs·2026
Same journal

Comparison of knockdown approaches for the generation of stable cell populations expressing afucosylated antibodies.

mAbs·2026
See all related articles

Related Experiment Video

Updated: Apr 16, 2026

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

8.4K

Boosting antibody developability through rational sequence optimization.

Daniel Seeliger1, Patrick Schulz, Tobias Litzenburger

  • 1a Division Research Germany; Boehringer Ingelheim Pharma GmbH & Co. KG ; Biberach/Riss , Germany.

Mabs
|March 12, 2015
PubMed
Summary
This summary is machine-generated.

Computational methods enhanced antibody stability and expression for therapeutic development. Sequence modifications improved in vitro properties, increasing the success rate for antibody therapeutics.

Keywords:
CMC, chemistry, manufacturing and controlDSC, differential scanning calorimetryHC, heavy chainLC, light chainPK, pharmacokineticsRALS, right angle light scatteringWT, wild-typebiopharmaceuticalsdesigndevelopabilitymAb, monoclonal antibodymonoclonal antibodiespredictionprotein engineeringstabilitythermal stability

More Related Videos

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

19.5K
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

Related Experiment Videos

Last Updated: Apr 16, 2026

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

8.4K
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

19.5K
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

Area of Science:

  • Biotechnology
  • Protein Engineering
  • Immunology

Background:

  • Monoclonal antibodies are crucial therapeutics, but their development is challenged by stability and property requirements.
  • Understanding the link between antibody protein sequence and in vitro properties is essential for successful therapeutic development.

Purpose of the Study:

  • To systematically modify an antibody with precipitation issues using computational design.
  • To improve the in vitro stability and expression levels of therapeutic antibodies.

Main Methods:

  • Employed heuristic sequence analysis and computational design strategies to modify antibody sequences.
  • Assessed antibody stability using biophysical methods and long-term stability experiments.
  • Evaluated expression levels of modified antibodies compared to the wild-type.

Main Results:

  • A series of modified antibodies demonstrated improved stability and reduced precipitation in vitro.
  • Expression levels of the optimized antibodies were notably higher than the wild-type candidate.
  • Experimental and computational data consistently supported the impact of introduced mutations on stability.

Conclusions:

  • Computational methods can effectively guide antibody sequence optimization for enhanced stability.
  • The developed approach improves the success rate of antibody therapeutics by addressing in vitro properties.
  • This strategy offers a pathway for engineering more robust and effective antibody-based medicines.