Design and evaluate in-solution affinity determination runs using non-modified substances
Developing monoclonal antibody-based therapeutics includes optimizing and monitoring their binding specificity and affinity to the target molecule. For example, therapeutic antibodies with high affinity have higher efficacy and reduce the risk of side effects. The demand for higher affinity and the use of newer affinity maturation techniques requires robust analytical methods that can accurately determine equilibrium dissociation constants (KD) in the low- or sub-picomolar range.
Measuring free fractions of interactants in equilibrated solutions with Gyrolab flow-through immunoassays provides unique advantages based on the short binding times for the affinity column. Short contact times of only a few seconds avoid the equilibrium shifts that are inherent in assays requiring long incubation times.
Gyrolab Affinity Software module facilitates the design and evaluation of in-solution affinity determination experiments. The software guides you in defining the interacting pairs and setting up the affinity sample series. At equilibrium, the response from the unbound interactant in each affinity sample is measured with an automated Gyrolab Affinity Analysis run, requiring sample volumes as small as 4 µL.
Affinity analysis results are available for review immediately after the assay is completed.
Learn about Gyrolab in-solution affinity analysis of ultra-high affinity, sub-nanomolar KD interactions. "Application of the Gyrolab microfluidic platform to measure picomolar affinity of a PD-L1-binding Adnectin™ radioligand for positron emission tomography."
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