Name: Introduction to single domain antibodies
Uploaded: 2022-09-12T00:00:00.0000000
Duration: T00H02M25S
Description: Introduction to single domain antibodies

Name: Introduction to single domain antibodies

Description: Introduction to single domain antibodies

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Upload Date: 2022-09-12T00:00:00.0000000

Transcript: Language: EN.
Segment:0 .
[MUSIC PLAYING]
BEATRICE BOWLBY: Single-domain antibodies, also known as VHH antibodies or nanobodies, are antibodies derived from camelids that have a single monomeric variable antibody domain. Single-domain antibodies were first discovered in 1989 by the Hamers' lab in Brussels, Belgium where they were researching treatments for infections in camels. Camels, llamas, and alpacas are all part of the camelid family, which produce both conventional antibodies, containing heavy and light chains, as well as heavy chain-only antibodies.
BEATRICE BOWLBY: Cloned from the heavy chain-only B cells of camelids, single-domain antibodies consist of only the binding domain of these heavy chains. This leads to a molecule of less than 15 kilodaltons in size, making them less than 1/10 the size of traditional antibodies. Single-domain antibodies unique small size, longer complementarity determining regions, access to hard-to-reach epitopes, and special structures offer several advantages.
BEATRICE BOWLBY: These advantages include greater tissue penetration, unique conformational epitope-specific recognition, high affinity and specificity, increased stability in extreme environments, cost-effective scale-up production, and a wide range of applications, including high-resolution imaging. Single-domain antibodies have become more accessible with pioneers, such as ProSci Inc, offering both products and custom antibody services to researchers worldwide.
BEATRICE BOWLBY: The process to develop these tools is like other recombinant antibody technologies, with antigen design and immunization followed by separating lymphocytes from whole blood and cDNA library construction. Libraries are then enriched via phage display to isolate highly specific and high-affinity antibody fragments against the target of interest. Once identified, bacterial expression in E coli is optimized to produce the antibody.
BEATRICE BOWLBY: With their unique characteristics, llama single-domain antibodies have become attractive tools for diagnostic tests, such as lateral flow assays and ELISA, developing therapeutics for cancer and infectious diseases, imaging, and other research applications, including crystallography and cryo-EM. To find out more about single-domain antibodies, check out our in focus with ProSci on www.biotechniques.com. [MUSIC PLAYING]

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