WEBINAR

Demonstrating Versatility of Single-Domain Antibodies In Antibody Therapeutics Development

April 1, 2021 | 11am EDT | 4pm BST | 5pm CEST
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During this presentation we will outline the versatility of these ligands and show examples of how they can be used for purification, quantification and characterization of different antibody formats.

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Webinar Summary

The family of Camelidae possess a unique repertoire of fully functional
antibodies, which are naturally devoid of light chains. Since the discovery of camelid heavy chain antibodies in the early 90’s, the use of their pared
down version, known as single domain antibodies (sdAbs) or VHH ligands, has seen a tremendous uptake in various fields.

sdAbs harbor the full antigen-binding capacity of the original heavy chain
antibody, but the small size (~12-15kD) enables them to reach epitopes
normally unavailable for conventional IgGs. These ligands bind their
targets with high affinity and selectivity. Due to their tunable specificity,
high stability and efficient production in low eukaryotic species, this
technology has been embraced by multiple disciplines of research and
medicine.

The CaptureSelect™ camelid single domain antibody technology has been
developed for the routine purification of a wide range of biologics,
including therapeutic antibodies and antibody fragments. In addition to
purification in drug development, sdAbs also have specific advantages
useful for the development of analytical methods.

During this presentation we will outline the versatility of these ligands and
show examples of how they can be used for purification, quantification
and characterization of different antibody formats.

Attend this webinar to discover:

  • The versatility of single domain antibody technology in antibody drug development
  • The sdAbs which help increase efficiency of antibody purification
  • The development of analytical methods based on sdAb technology

Speaker Information:


WebinarSpeakerImage
Pim Hermans
Head of Ligand Discovery
Thermo Fisher Scientific