Antibody Affinity Determination Service

Tek Biotech has been committed to the study of interactions between biomolecules for many years. Interaction studies of biological molecules such as nucleic acids, proteins and viruses and understanding their mechanism of action and functional mechanism is the current hotspot of life science research. Affinity is an important parameter to judge the interaction between molecules, and it is an important index to understand molecules as well as the discovery and screening of drugs, etc. Our scientific research experts have accumulated many years of experience in interactions research and testing, and we can provide customers with high-quality affinity determination service by virtue of our rich experience in technology, and we insist on the fine control of each experimental step to ensure the smooth progress of customers' experiments.

Affinity is a characteristic parameter for evaluating the strength of interaction between two molecules in the process of reversible reaction, and it is an important index for understanding molecules as well as recognizing the biological process, drug discovery and screening. It is of great significance in the early research and development of drugs, screening and identification, as well as downstream production quality control, and it is also widely used in the basic research of life sciences and the development of biopharmaceuticals. Relying on a well-established platform, Tek Biotech is committed to providing customers with high-quality one-stop technical services to meet the experimental needs of different customers.

█ Type of Service

Based on Octet and Biacore platforms, Tek Biotech provides customers with accurate and rapid affinity determination services, as well as distinctive intermolecular interaction analysis services according to customers' needs, including but not limited to the commonly used techniques in the industry: Surface Plasmon Resonance (SPR) and Bio-Layer Interferometry (BLI) to ensure accurate, objective and credible results. Bio-Layer Interferometry (BLI) to ensure accurate, objective and reliable results. We strive to provide accurate testing services to meet the needs of different customers.

   BLI affinity Determination: An optical analytical technique that detects changes in the thickness of the surface layer of a biomolecule immobilized on a biosensor. If the molecule to be measured binds to the immobilized molecules on the tip of the biosensor, the change in their number can lead to a corresponding change in the interferogram measured in real time, thus obtaining information on intermolecular interactions.

   Fig3. Receptor protein and small molecule BLI Determination results

   SPR affinity determination: by fixing a molecule on the surface of the sensing chip in the form of another molecule in the form of a solution flowing continuously through the chip, the detector can detect in real time the molecules in the solution and the molecules on the surface of the chip in the process of binding and dissociation.SPR monitors the information of intermolecular interactions in real time by real-time recording of the changes in the molecular mass of the molecule on the surface of the sensor chip.

   Fig4. Receptor protein and small molecule SPR Determination results

█ Significance of Affinity Measurements

IC50: Usually refers to the half-inhibitory concentration (or half-inhibitory rate), or IC50, the concentration of drug or inhibitor required to inhibit a specified biological process (or a component of that process such as an enzyme, receptor, cell, etc.) by half. Used in pharmacology to characterize the antagonist's (antagonist) ability to antagonize in in vitro experiments (in vitro).

EC50: The concentration of a drug, antibody or toxin that achieves 50% of its maximum biological effect after a specific exposure time. In pharmacology, in addition to characterizing the activating ability of an agonist in vitro, it is also used to indicate the blood concentration required to reach half of the maximum biological effect in vivo.

K_D: dissociation constant, the concentration of free inhibitor that corresponds to 50% of enzyme E bound by inhibitor I. It can be used in some cases in conjunction with K_I to indicate the blood concentration required to achieve half of the maximum biological effect in vivo. In some cases, it can be equated with K_I. K_D is generally measured by SPR and other experiments, usually without the presence of a substrate, while K_I is measured with the simultaneous presence of a substrate, which competes for the substrate. Therefore, K_I is generally measured at a greater concentration than K_D.

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 █ Service Advantages

-- Diversified testing platforms to meet different testing needs

-- Highly accurate analyzers, experienced operators and strict quality control ensure accurate and reliable results.

-- High detection efficiency, no need for labeling, high throughput detection, real-time monitoring of the detection process.

-- Convenient method design, simple, flexible and easy to operate.

-- Higher detection sensitivity and lower sample consumption.

-- Strong anti-interference ability: the detection is not affected by temperature, refractive index of buffer and other external environment.

-- Wide range of applications: can be used for molecular interaction analysis of proteins, nucleic acids, peptides, nanomaterials, etc.

-- Provide a true one-stop service experience: provide an integrated solution from affinity determination service to molecular interactions research.