Measuring Affinity & Kinetics: The essential guide to understanding KinExA technology & high-affinity binding
September 21-22, 2023
​Boise, Idaho

- Speakers from Amgen, Bristol Meyers Squibb, Xavier University, & more -
- In-depth training workshops with Sapidyne scientists -
- Learn to streamline your experimental design & data analysis -
- Gain a better understanding of KinExA Pro software -
- Learn how to apply the Theory Curve to your research -
- Go in-depth on using KinExA to characterize membrane protein targets -

Agenda

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The only biosensor available that can accurately measure binding interactions from nM to fM. 

Equilibrium Dissociation Constant (Kd)
Association Rate Constant (Kon)
​Dissociation Rate Constant (Koff)
Concentration Immunoassay

For over 25 years KinExA® Technology has been used to detect & measure biological interactions in the most physiologically relevant conditions. 

KinExA instruments are easy to use and require no expensive consumables like chips, plates, or kits to run experiments.

If you are using SPR, BLI, or LSA, you need KinExA to identify and optimize your lead candidates. KinExA instruments overcome the limit of detection and immobilization presented by other technologies.

Trusted Accuracy | Proven Reliability | Unrivaled Sensitivity

The KinExA Advantage - A Comparison of Biosensors

" By tailoring the KinExA to each studied antigen, we obtained apparent equilibrium dissociation constants (Kd values) spanning six orders of magnitude, from approximately 100 fM to 100 nM. " 
Bee C. et. al. 2012 Exploring the dynamic range of the kinetic exclusion assay in characterizing antigen-antibody interactions.
​PLOS ONE 7(4) ​http://www.ncbi.nlm.nih.gov/pubmed/22558410

" The kinetics of binding and affinity of the 4 chimeric clones to human IL-21 were determined using a kinetic exclusion assay (KinExA)...Among the four lead clones, 19E3 had the highest affinity to recombinant human IL-21 of 243 fM " 
Reena Varkey et. al. 2019 Discovery and characterization of potent IL-21 neutralizing antibodies via a novel alternating antigen immunization and humanization strategy. PLOS ONE  
https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0211236

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