Affinity Characterization
Last updated
Last updated
Affinity characterization offers a detailed and quantitative analysis of the interactions between protein variants and their target. By measuring binding events at multiple concentrations, this assay provides accurate kinetic constants, including the association rate constant (k_on), dissociation rate constant (k_off), and equilibrium dissociation constant (K_D). These high-resolution kinetics are critical for understanding the strength, speed, and stability of protein-target interactions.
Under normal conditions, our system can quantify KD values in the range of 0.1 nM to 10 μM.
Key Features:
Starts at 149$/protein. 21 days turnaround time.
Precise Kinetics: Accurate measurements of k_on, k_off, and K_D provide a complete picture of binding behavior. KD values are in the range of 0.1 nM to 10 μM
Multi-Concentration Analysis: Measurements across multiple concentrations enhance data reliability and precision.
When to Use:
After initial screening has identified promising binders.
When precise binding kinetics are required for optimization or selection.
To validate lead candidates prior to downstream applications.
Affinity measurements depend heavily on selecting the correct concentration range for both the target and the analyte. Adaptyv employs a preliminary optimization phase to identify the ideal range, ensuring robust signals without excessive noise or non-specific binding. Typical concentration ranges include:
High-Affinity Binders: Measured at lower concentrations (e.g., nanomolar ranges).
Weaker Binders: Require higher concentrations (e.g., micromolar ranges). This optimization ensures the accuracy and reproducibility of derived kinetic constants, even for complex or low-affinity interactions.
