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

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Antibody Affinity Maturation Service

Antibody binding affinity is one of the key parameters that determine the efficacy and dosage of antibody drugs. Currently, methods to improve antibody binding affinity are focused on site mutation, CDR rearrangement, and DNA recombination. With our effective antibody affinity maturation technology, we can rapidly discover key amino acid sites in antibody domains. This in turn increases the binding affinity of the antibody to at least the nM level.

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█ Service Content

Content	Deliveries	Period
DNA reorganization	Antibody Sequence and Sequencing Report 1-3 of optimized antibodies Full Analysis Report (PDF)	24-28 weeks
Library Construction and Screening
Antibody Production and Validation

█ Benefits of Phage-based Selection

Phage selection is very versatile and can be customized to obtain the desired antigen specificity or affinity parameters. Options include:

(1) Negative selection for cross-reactive binders by competing with a negative control antigen

(2) kinetic selection based on dissociation rate by encapsulating antigen at lower concentrations or by varying incubation and wash times

(3) Antigen conformation-specific selection compatible with recombinant and cell-based antigens

(4) Final phage viruses are stable at 80°C, allowing selection of heat-stable, highly expressed clones

We perform rapid screening after phage panning, and after selection, hundreds of randomly selected clones are generated and screened for soluble Fab from bacterial supernatants. screening lead candidates at high throughput saves significant time and resources before moving on to the time-consuming phase of IgG production. In addition to full sequence analysis, recombinant or cell-based proteins can be screened in high throughput by ELISA, flow cytometry, functional assays and BLI.

█ Service Advantages

-- Effective random mutagenesis through DNA reorganization

-- Mature phage display platform to ensure high-quality antibody affinity maturation services

-- Affinity assessment

Antibody Affinity Maturation Service Frequently Asked Questions

Q: The low expression level of bispecific antibodies in the host system leads to insufficient production.

A: Optimize the construction of expression vectors, including selecting appropriate promoters, signal sequences, and host systems; Optimize cultivation conditions, such as temperature, medium composition, oxygen supply, etc., to increase expression levels; Consider using enhancers or expression adjuvants to improve the expression efficiency of antibodies.
Q: The structure or activity of bispecific antibodies is affected, resulting in incomplete function or inability to express them normally.

A: Optimize the design of antibody structure to ensure its correct conformation and function; Evaluate the activity and stability of bispecific antibodies through structural prediction and analysis; Perform functional validation to confirm the activity and specificity of the antibody.
Q: The selection and design of antigens may affect the binding efficiency and specificity of bispecific antibodies.

A: Optimize the design and expression of antigens to ensure their binding efficiency and specificity with bispecific antibodies; Conduct preliminary antigen assessment and screening to select the most suitable antigen; Consider using affinity modification or structural optimization methods to improve the binding efficiency and specificity between antibodies and antigens.
Q: The purification and stability of bispecific antibodies may be affected, affecting the reliability of subsequent applications.

A: Optimize purification methods and steps, select appropriate purification columns, chromatography conditions, and elution buffer to improve purification efficiency; Conduct stability testing to evaluate the stability and storage conditions of antibodies; Consider using additives or protectants to improve the stability and shelf life of antibodies.
Q: The affinity of antibodies is insufficient, resulting in weak binding ability with the target.

A: Using various techniques for affinity maturation, such as tandem mutagenesis, DNA ethylation, RNA aptamer technology, etc; Using a screening library for high-throughput screening, selecting mutants with high affinity; Conduct structural analysis to explore potential mechanisms for enhancing affinity.
Q: Antibodies may undergo non-specific binding during maturation, binding to non target proteins.

A: Perform specific screening to identify mutants with high affinity and low non-specific binding to the target protein; Optimize the selection criteria and improve the specificity of screening; Design using binding site information to reduce non-specific binding.
Q: The structural stability of antibodies may be affected, affecting their stability under physiological conditions.

A: By constructing a mutation library, we can screen out mutants with more stable structures; Optimizing the antibody framework using protein engineering technology to enhance its structural stability; Conduct structural analysis to understand the impact of mutations on structural stability.

Q: The low expression level of bispecific antibodies in the host system leads to insufficient production.

A: Optimize the construction of expression vectors, including selecting appropriate promoters, signal sequences, and host systems; Optimize cultivation conditions, such as temperature, medium composition, oxygen supply, etc., to increase expression levels; Consider using enhancers or expression adjuvants to improve the expression efficiency of antibodies.
Q: The structure or activity of bispecific antibodies is affected, resulting in incomplete function or inability to express them normally.

A: Optimize the design of antibody structure to ensure its correct conformation and function; Evaluate the activity and stability of bispecific antibodies through structural prediction and analysis; Perform functional validation to confirm the activity and specificity of the antibody.
Q: The selection and design of antigens may affect the binding efficiency and specificity of bispecific antibodies.

A: Optimize the design and expression of antigens to ensure their binding efficiency and specificity with bispecific antibodies; Conduct preliminary antigen assessment and screening to select the most suitable antigen; Consider using affinity modification or structural optimization methods to improve the binding efficiency and specificity between antibodies and antigens.
Q: The purification and stability of bispecific antibodies may be affected, affecting the reliability of subsequent applications.

A: Optimize purification methods and steps, select appropriate purification columns, chromatography conditions, and elution buffer to improve purification efficiency; Conduct stability testing to evaluate the stability and storage conditions of antibodies; Consider using additives or protectants to improve the stability and shelf life of antibodies.
Q: The affinity of antibodies is insufficient, resulting in weak binding ability with the target.

A: Using various techniques for affinity maturation, such as tandem mutagenesis, DNA ethylation, RNA aptamer technology, etc; Using a screening library for high-throughput screening, selecting mutants with high affinity; Conduct structural analysis to explore potential mechanisms for enhancing affinity.
Q: Antibodies may undergo non-specific binding during maturation, binding to non target proteins.

A: Perform specific screening to identify mutants with high affinity and low non-specific binding to the target protein; Optimize the selection criteria and improve the specificity of screening; Design using binding site information to reduce non-specific binding.
Q: The structural stability of antibodies may be affected, affecting their stability under physiological conditions.

A: By constructing a mutation library, we can screen out mutants with more stable structures; Optimizing the antibody framework using protein engineering technology to enhance its structural stability; Conduct structural analysis to understand the impact of mutations on structural stability.

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Antibody Affinity Maturation Service Frequently Asked Questions

Q: The low expression level of bispecific antibodies in the host system leads to insufficient production.

Q: The structure or activity of bispecific antibodies is affected, resulting in incomplete function or inability to express them normally.

Q: The selection and design of antigens may affect the binding efficiency and specificity of bispecific antibodies.

Q: The purification and stability of bispecific antibodies may be affected, affecting the reliability of subsequent applications.

Q: The affinity of antibodies is insufficient, resulting in weak binding ability with the target.

Q: Antibodies may undergo non-specific binding during maturation, binding to non target proteins.

Q: The structural stability of antibodies may be affected, affecting their stability under physiological conditions.