Affinity Measurement

To determine the kinetic properties of antibody-antigen interactions, Creative Biolabs employs various platforms to measure the affinity of the antibody or protein for the corresponding ligand which is critically important for understanding your molecule.

Affinity Measurement Services

Antibody and antigen interactions are reversible and non-covalent which is formed by a combination of hydrophobic interactions, electrostatic and Vander Waals forces, and hydrogen bonds. The strength of antibody/antigen interactions is measured to determine the affinity which is defined by the basic thermodynamic principles. Any reversible biomolecular interaction follows this principle (see Fig.1).

Our one-stop solution flow chart. Fig.1 Affinity of the interaction.

With extensive experience in measuring the kinetic and binding affinity of protein, Creative Biolabs has developed the following technologies for your flexible choices to best fit your project.

Platform Services
Industry leading Biacore T200 platform
  • Determining protein interactions.
Surface Plasmon Resonance (SPR) technology
  • Real-time measurement of label-free antibody/target interactions;
  • Determining antigen affinity constants;
  • A broad range of kinetic binding parameters such as Kd, Ka can be determined;
  • Can be used for proteins expressed in crude periplasmic extracts.
BLI-based Octet system
  • Kinetic properties of antibody/antigen interactions.

SPR measurements can also be applied in the following assays, in addition to determining the kinetic affinity.

Stand-alone activity or an integrated comprehensive service are both welcomed at Creative Biolabs.

Single cycle kinetics

A series of analyte concentrations are run in one cycle, and there is no regeneration between sample injections. We offer this kind of valuable approach when acceptable regeneration cannot be achieved. It’s also useful in screening many variants in a single assay, and it allows ranking of variants compared with original molecule.

Multicycle kinetics

Different with single cycle kinetics, multicycle kinetics runs each analyte concentration in different cycles. The surface is regenerated after each sample dissociation. The advantage of this approach is consistent surface properties between cycles which is important to optimize the regeneration. Once performed, accurate Ka, Kd and KD values will be provided.

Evaluation of kinetic titration series (A) and parallel sensor kinetics (B) with IgG binding to GB1 in BLI. Fig.2 Evaluation of kinetic titration series (A) and parallel sensor kinetics (B) with IgG binding to GB1 in BLI. (Frenzel, 2014)

With advanced platforms and senior scientists, Creative Biolabs is fully competent for performing antibody affinity and kinetic measurement which enable determining molecular interactions in a real-time manner. All data will be analyzed and documented in the final report for delivery. For more information, please don’t hesitate to contact us.

Reference

  1. Frenzel, D. and Willbold, D. Kinetic titration series with biolayer interferometry. PLoS One. 2014, Sep 17;9(9).

For Research Use Only | Not For Clinical Use

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