×

Learn more

First Name
Last Name
Company Name
Country
State
Province
State
Region
State
Canton
Yes, keep me updated about NanoTemper
By checking this box, you provide us consent to email you educational content, and information on our products, services and events. You may unsubscribe at any time.
Agree to Privacy Policy*
*I have fully read, understood and agree to the Privacy Policy. I accept the storing and processing of my personal data by NanoTemper as described in the Privacy Policy.
Thank you!
Error - something went wrong!
   

Using MST to analyse the binding of nanobodies and nanobody-Fc fusion proteins to human CD38

Abstract: Antibody affinities play an important role in diagnostic, basic research and medical applications. Conventional antibodies are composed of two heavy and two light chains. Both chains contribute to binding of the antigen by their variable domains. In addition to conventional antibodies, llamas produce functional heavy chain antibodies that lack light chains and interact with antigens solely via the variable domain of the heavy chain, designated VHH. Recombinant VHHs are also called single domain antibodies or Nanobodies because of their size in the nm range. In this study we compared the binding of Nanobodies and Nanobody-Fc fusion proteins to human CD38 using Microscale Thermophoresis (MST). This study highlights the potential of MST-Technology in affinity determination of antibody-antigen interactions.​

 

Previous
Using MST to analyse the binding of the β-Lactamase TEM1 to BLIP
Using MST to analyse the binding of the β-Lactamase TEM1 to BLIP

Next
Binding of histone peptides to chromatin assembly factor I (CAF-I) p48 subunit
Binding of histone peptides to chromatin assembly factor I (CAF-I) p48 subunit

Have a question?

Contact Specialist