Affinity Measurement

Affinity Measurement

Affinity Measurement Principle 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 is measured by basic thermodynamic principles.

Our Affinity Measurement Techniques Platforms

Services

Industry Leading Biacore T200 Platform

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Determining protein interactions.

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Real-time measurement of label-free antibody/target interactions;

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Determining antigen affinity constants;

Surface Plasmon Resonance (SPR) Technology

Bio-layer Interferometry (BLI)based Octet System

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A broad range of kinetic binding parameters such as Kd, Ka can be determined;

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Can be used for proteins expressed in crude periplasmic extracts.

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Kinetic properties of antibody/antigen interactions.

Single cycle kinetics -- It’s offered when acceptable regeneration cannot be achieved. It’s also useful in screening many variants in a single assay, and allows ranking of variants compared with original molecule.

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Multicycle kinetics -- The advantage is consistent surface properties between cycles. Once performed, accurate Ka, Kd and KD values will be obtained.

Creative Biolabs Confidential

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