Antibody Affinity Determination Service-Tekbiotech-Yeast Display Service,Phage display technology

Services

Inquiry and ordering

Name*
Phone*
Email*
Product*
Content*

Antibody Affinity Determination Service

Over the years, TekBiotech has accumulated more than 10,000+ biomolecular affinity measurement services. Affinity is a characteristic parameter for evaluating the strength of the interaction between two molecules in a reversible reaction process. It is an important indicator for understanding molecules and identifying biological processes, drug discovery and screening, etc. It is of great significance in early drug research and development, screening and identification, and downstream production quality control, and is also widely used in basic research in life sciences, biopharmaceutical development and other fields. Relying on the construction of a complete platform, TekBiotech focuses on providing customers with high-quality one-stop technical services to meet the experimental needs of different customers.

█ Affinity Measurement Service Method

TekBiotech provides customers with accurate and rapid affinity measurement services based on platforms such as Octet and Biacore, and provides unique molecular interaction analysis services according to customer needs, including but not limited to commonly used detection technologies in the industry: surface plasmon resonance (SPR) and bio-layer interferometry (BLI), to ensure that the test results are accurate, objective and reliable. We focus on providing customers with accurate detection services to meet the experimental needs of different customers.


Figure1 SPR determination (Biacore-T200)	Figure2 BLI determination (ForteBio Octet)

(1) SPR Affinity Determination:

SPR affinity determination is a method of fixing one molecule on the surface of a sensor chip and continuously flowing another molecule through the chip in the form of a solution. The detector can detect the binding and dissociation process between the molecule in the solution and the molecule on the chip surface in real time. SPR monitors the interaction information between molecules in real time by recording the change in molecular mass on the surface of the sensor chip in real time.

Antibody Affinity Measurement Service-tekbiotech3.png

Figure3 SPR detection results of receptor proteins and small molecules

(2) BLI Affinity Determination:

BLI affinity determination is an optical analysis technology that detects changes in the thickness of the surface layer of biomolecules fixed on the biosensor. If the molecule to be tested binds to the fixed phase molecule at the tip of the biosensor, the change in its quantity can cause a corresponding change in the interference pattern measured in real time, thereby obtaining information on the interaction between molecules.

Antibody Affinity Measurement Service-tekbiotech4.png

Figure4 BLI test results of receptor protein and small molecule

Although the SPR and BLI methods are different in principle, the data finally obtained in the experimental detection process are comparable, and both can obtain Kd, K_off and K_on values. The BLI method has a wider range of requirements for buffer than the SPR method, and is more suitable for rapid scanning of the binding ability between small molecules and proteins, with a higher cost-effectiveness. In addition, TekBiotech also provides customers with EC50 data determination based on the ELISA method, which can effectively save the cost and time of rapid screening of targeted antibody drugs.

█ Sample Requirements for Affinity Determination Service

Sample Type

Requirements

Antibodies, proteins, peptides, small molecules, etc.

* Buffer: PBS, HEPPS, etc., without organic reagents, without Tris, EDTA or DDT;

* Protein sample (including antibody): 200ug, concentration>0.5mg/ml;

* Peptide sample: 200ug, concentration>1mg/ml;

* Small molecules: 1mg, concentration>1mg/ml, purity>90%, dissolved in 100% DMSO or water.

█ Affinity Measurement Service Advantages

Diversified testing platforms to meet

different testing needs

Pre-CNAS testing certification system

Wide range of applications: can be used

for molecular interaction analysis of

proteins, nucleic acids, polypeptides,

nanomaterials, etc.

Provide a truly one-stop service

experience: provide integrated

solutions from affinity measurement

services to molecular interaction research

Antibody Affinity Determination Service Frequently Asked Questions

What is Antibody Affinity Assay? Why is antibody affinity so important?

Antibody affinity assay is the process of quantifying the strength of binding between an antibody and its target (e.g., antigen) through a series of experimental methods. Affinity usually refers to how tightly an antibody binds to an antigen and is often expressed as a dissociation constant (Kd). Affinity is critical to the function of an antibody because it determines the ability of an antibody to bind to an antigen and its biological effects. Higher affinity usually means that the antibody recognizes and binds the antigen more efficiently, thus enhancing the immune response or drug efficacy. In the development of antibody drugs, affinity determination is the basis for ensuring the effectiveness and selectivity of antibody drugs. Antibodies with high affinity can effectively target disease-related molecules, reducing off-target effects and enhancing therapeutic efficacy. In addition, affinity also determines the stability, clearance and pharmacokinetic properties of the antibody, which are critical to the efficacy and safety of clinical therapy. Therefore, accurate determination of antibody affinity is essential for optimizing antibody development and clinical application.
What are the common methods for antibody affinity determination?

1), Surface Plasmon Resonance (SPR): SPR is a very sensitive real-time assay that can directly measure the binding kinetics (e.g., binding rate and dissociation rate) between an antibody and an antigen. By this method, the affinity constant (Kd) of the antibody can be calculated, and the method does not require labeling of the antibody or antigen, which makes it suitable for high-throughput screening.2), Enzyme-linked immunosorbent assay (ELISA): ELISA is one of the most common affinity assays, in which the affinity is estimated by measuring the intensity of the signal generated by the antibody binding to the antigen (e.g., enzyme-labeled substrate reaction). ELISA is suitable for quantitative analysis of the affinity of antibodies, but it requires calculations to deduce the dissociation constant and is not as sensitive as SPR. 3) Isothermal titration calorimetry (ITC): ITC can directly measure the thermal effect of the binding process of antibodies to antigens, thus obtaining information on the affinity, binding sites, etc. ITC provides a very accurate method of determining the affinity, but is more complicated to operate and is usually 4) Competition binding assay: affinity can also be calculated by determining the ability of antibodies to compete for binding with different concentrations of antigen. This method is suitable for specific experimental designs, especially when screening antibodies in complex samples.
How does the dissociation constant (Kd) of an antibody affinity assay affect the therapeutic effect of a drug?

The dissociation constant (Kd) of an antibody affinity assay is a key indicator of the stability of an antibody's binding to an antigen. the smaller the Kd value, the stronger the affinity of the antibody to bind to the antigen, and the more tightly it binds. For the therapeutic efficacy of antibody drugs, a lower Kd value usually means that the antibody is able to effectively bind to the target at low concentrations and continuously maintain this binding state, thus enhancing the efficacy of the drug. Antibodies with high affinity can improve the precision and selectivity of targeted therapies, reduce interference with non-target tissues, and decrease side effects. On the other hand, a low Kd value may cause problems, such as rapid clearance of the drug or side effects such as “antibody-dependent cytotoxicity” (ADCC) due to overly efficient binding. Therefore, drug developers need to find an optimal affinity range through affinity assays so that the antibody can target the antigen efficiently while maintaining appropriate pharmacokinetic properties in vivo. In conclusion, the precise determination and regulation of antibody affinity is an important means to improve the therapeutic effect of antibody drugs and reduce side effects.
Can antibody affinity assay detect the diversity of antibody-antigen reactions?

Antibody affinity assays can be used not only to assess the strength of antibody-antigen binding, but also to provide researchers with valuable information about the diversity of antibody-antigen reactions by analyzing binding kinetics (e.g., binding and dissociation rates). In complex antigen systems, antibodies may interact with multiple epitopes or subepitopes to produce different binding modes. These different reaction patterns can be identified and the affinity of the different reactions can be quantified by antibody affinity measurements, especially using surface plasmon resonance (SPR) techniques. Specifically, the reaction of an antibody with an antigen may occur at a number of different binding sites, resulting in a variety of different binding states. This diversity may affect the efficacy and therapeutic effectiveness of the antibody. For example, some antibodies may be able to recognize multiple epitopes of an antigen at the same time, producing a synergistic effect that enhances the antibody's effect. Other antibodies, on the other hand, may have high affinity for only specific epitopes and thus exhibit different biological activities. Through detailed determination of antibody affinity, researchers are able to assess the diversity of antibody-antigen responses and select the most clinically promising antibody candidates for further development. Thus, antibody affinity assays not only help developers screen for the best antibodies, but also provide powerful support for a deeper understanding of antibody-antigen interactions.
How does the antibody affinity assay service help in antibody screening and drug development?

Antibody affinity assay services play a central role in antibody screening and drug development. First, affinity assays can help screen for the antibody that binds most tightly to the target, thereby ensuring its effectiveness in subsequent development and reducing costs and time. Secondly, affinity assays provide data support for antibody optimization, helping to identify the best binding characteristics, optimize antibody structure, and enhance drug efficacy. In addition, affinity assays can assess the stability and half-life of antibodies, optimize pharmacokinetic properties, and enhance drug performance in vivo. Therefore, affinity assay service is an indispensable tool for antibody screening, optimization and drug development, which greatly facilitates the successful development of antibody drugs.

What is Antibody Affinity Assay? Why is antibody affinity so important?

Antibody affinity assay is the process of quantifying the strength of binding between an antibody and its target (e.g., antigen) through a series of experimental methods. Affinity usually refers to how tightly an antibody binds to an antigen and is often expressed as a dissociation constant (Kd). Affinity is critical to the function of an antibody because it determines the ability of an antibody to bind to an antigen and its biological effects. Higher affinity usually means that the antibody recognizes and binds the antigen more efficiently, thus enhancing the immune response or drug efficacy. In the development of antibody drugs, affinity determination is the basis for ensuring the effectiveness and selectivity of antibody drugs. Antibodies with high affinity can effectively target disease-related molecules, reducing off-target effects and enhancing therapeutic efficacy. In addition, affinity also determines the stability, clearance and pharmacokinetic properties of the antibody, which are critical to the efficacy and safety of clinical therapy. Therefore, accurate determination of antibody affinity is essential for optimizing antibody development and clinical application.
What are the common methods for antibody affinity determination?

1), Surface Plasmon Resonance (SPR): SPR is a very sensitive real-time assay that can directly measure the binding kinetics (e.g., binding rate and dissociation rate) between an antibody and an antigen. By this method, the affinity constant (Kd) of the antibody can be calculated, and the method does not require labeling of the antibody or antigen, which makes it suitable for high-throughput screening.2), Enzyme-linked immunosorbent assay (ELISA): ELISA is one of the most common affinity assays, in which the affinity is estimated by measuring the intensity of the signal generated by the antibody binding to the antigen (e.g., enzyme-labeled substrate reaction). ELISA is suitable for quantitative analysis of the affinity of antibodies, but it requires calculations to deduce the dissociation constant and is not as sensitive as SPR. 3) Isothermal titration calorimetry (ITC): ITC can directly measure the thermal effect of the binding process of antibodies to antigens, thus obtaining information on the affinity, binding sites, etc. ITC provides a very accurate method of determining the affinity, but is more complicated to operate and is usually 4) Competition binding assay: affinity can also be calculated by determining the ability of antibodies to compete for binding with different concentrations of antigen. This method is suitable for specific experimental designs, especially when screening antibodies in complex samples.
How does the dissociation constant (Kd) of an antibody affinity assay affect the therapeutic effect of a drug?

The dissociation constant (Kd) of an antibody affinity assay is a key indicator of the stability of an antibody's binding to an antigen. the smaller the Kd value, the stronger the affinity of the antibody to bind to the antigen, and the more tightly it binds. For the therapeutic efficacy of antibody drugs, a lower Kd value usually means that the antibody is able to effectively bind to the target at low concentrations and continuously maintain this binding state, thus enhancing the efficacy of the drug. Antibodies with high affinity can improve the precision and selectivity of targeted therapies, reduce interference with non-target tissues, and decrease side effects. On the other hand, a low Kd value may cause problems, such as rapid clearance of the drug or side effects such as “antibody-dependent cytotoxicity” (ADCC) due to overly efficient binding. Therefore, drug developers need to find an optimal affinity range through affinity assays so that the antibody can target the antigen efficiently while maintaining appropriate pharmacokinetic properties in vivo. In conclusion, the precise determination and regulation of antibody affinity is an important means to improve the therapeutic effect of antibody drugs and reduce side effects.
Can antibody affinity assay detect the diversity of antibody-antigen reactions?

Antibody affinity assays can be used not only to assess the strength of antibody-antigen binding, but also to provide researchers with valuable information about the diversity of antibody-antigen reactions by analyzing binding kinetics (e.g., binding and dissociation rates). In complex antigen systems, antibodies may interact with multiple epitopes or subepitopes to produce different binding modes. These different reaction patterns can be identified and the affinity of the different reactions can be quantified by antibody affinity measurements, especially using surface plasmon resonance (SPR) techniques. Specifically, the reaction of an antibody with an antigen may occur at a number of different binding sites, resulting in a variety of different binding states. This diversity may affect the efficacy and therapeutic effectiveness of the antibody. For example, some antibodies may be able to recognize multiple epitopes of an antigen at the same time, producing a synergistic effect that enhances the antibody's effect. Other antibodies, on the other hand, may have high affinity for only specific epitopes and thus exhibit different biological activities. Through detailed determination of antibody affinity, researchers are able to assess the diversity of antibody-antigen responses and select the most clinically promising antibody candidates for further development. Thus, antibody affinity assays not only help developers screen for the best antibodies, but also provide powerful support for a deeper understanding of antibody-antigen interactions.
How does the antibody affinity assay service help in antibody screening and drug development?

Antibody affinity assay services play a central role in antibody screening and drug development. First, affinity assays can help screen for the antibody that binds most tightly to the target, thereby ensuring its effectiveness in subsequent development and reducing costs and time. Secondly, affinity assays provide data support for antibody optimization, helping to identify the best binding characteristics, optimize antibody structure, and enhance drug efficacy. In addition, affinity assays can assess the stability and half-life of antibodies, optimize pharmacokinetic properties, and enhance drug performance in vivo. Therefore, affinity assay service is an indispensable tool for antibody screening, optimization and drug development, which greatly facilitates the successful development of antibody drugs.

Consult Now Antibody Affinity Determination Service