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Recombinant Fragment Antibody Customization Service

Antibodies/antibody fragments produce specific and efficient binding properties to antigens and play irreplaceable roles in biochemical, therapeutic and diagnostic fields. The traditional hybridoma technology for the production of monoclonal antibodies has become a bottleneck for the large-scale and rapid production of antibodies/antibody fragments due to its own relatively long research and development cycle and the relatively high cost of production. In recent years, with the continuous progress of genetic recombination and bioengineering technology, high-throughput screening and large-scale production of antibodies/antibodyfragments have become a reality.

Antigen-binding fragment (Fab) is the region on the antibody that binds to the antigen. It contains a constant region and a variable region for each heavy and light chain. Only the variable regions of the heavy and light chains are fused together to form a single-chain variable fragment (scFv), which is half the size of the Fab fragment but retains its original specificity. Another type of small antibody fragment, single domain antibody, also known as domain antibody, VHH, VNAR or sdAb, is an antibody fragment consisting of a single monomeric variable antibody structural domain lacking the conventional light and heavy chain CH structural domains.

Tek Biotech is a professional CRO service provider, which can provide our customers with high quality recombinant antibody expression services, such as scfv antibody fragment, fab antibody fragment, sdAb single domain antibody, heavy chain antibody and other recombinant antibody construction and expression services. In addition, Tek Biotech is currently building a 5,000 square meters GMP research center, which is capable of providing batch recombinant antibody production services for various industrial customers.

█ Antibody Fragment Characterization

Recombinant Fragment Antibody Customization Service.jpg

Antibody Type	Components	Molecular weight (kDa)	Valence (chemistry)	Half-life (h)
Fab	VH+CH1+VL+CL (light and heavy chains linked using disulfide bonds)	50-55	Monomers	12-20
scFv	VH+VL	30	Monomers	2-4
sdAb	VHH	15	Monomers	0.5
Fc Fusion Antibody	（ antibody+CH2+CH3）*2	/	Dimer	/
di-scFv	scFv*2	60	Dimer	4-8

█ Antibody Fragment Expression System Common Hosts

Expression System	Strain/Cell	Specificities
E.coli	BL21（DE3）	Ion-ompT，which effectively prevents intracellular hydrolysis of recombinant proteins
E.coli	Rosetta	The Rosetta (DE3) strain contains the pRARE plasmid, which is chloramphenicol-resistant and provides tRNAs for the rare codons of AUA, AGG, AGA, CUA, CCC, and GGA, which provides more “universal” protein expression and thus enhances the expression of target proteins.
Mammalian Cell	CHO-S	A commonly used cell line in the laboratory, grows well as an adherent wall and suspension culture with high productivity, ideal for large-scale cultures and GMP procedures; can be subjected to many post-translational modifications to obtain biosimilars, displaying excellent biocompatibility and drug activity; is suitable for protein-free, animal-production-free, and serum-free culture conditions, and offers improved stability and safety.
	CHO-K1
	Freestyle 293F	A class of wild-type 293 cell lines capable of highly expressing proteins in the absence of serum with high efficiency.
	Expi 293F	Has a highly transfectable line, demonstrates high protein expression levels, and exhibits more rapid cell growth and higher culture survival than standard suspension-adapted 293 cells.

█ Antibody Fragment High Expression Strategy

Optimization method	Characterization
Fusion Antibody	When Fab gene is expressed, the Fd gene and L chain gene, which carry the bacterial protein signal peptide gene at the 5' end, can be expressed in the periplasmic lumen of the E. coli cell wall in an endocrine fashion, forming a complete stereo-fold.The Fab fragment retains the antigen-binding specificity and biological activity of the parental antibody.The Fd gene fragment and L chain gene can be constructed in two vectors separately and then cotransfected into the cells, or they can be constructed in one vector to transfect cells for expression.
Modification of the Antibody Sequence Itself	Upon targeted mutagenesis, the amino acids of the antibody at certain key sites can be altered to optimize its stability, enhance its affinity for the antigen, and increase its expression yield.
Selection of Expression Systems	Factors that should be considered are: experimental equipment, toxicity of the antibody to be expressed, nutrients required, the need for high antibody yields, antibody purification processes, production costs, regulatory elements, and biosafety aspects.
Codon Optimization	Natural antibodies/scFv are derived from eukaryotic organisms, whose codons are most likely not preferred by E.coli. The use of preferred codons improves cellular adaptation to the environment and the antibody, and reduces the misfolding rate of recombinant antibodies.
Conditional Optimization	Factors to be considered include temperature, medium ratio, pH, incubation time and induction conditions.

█ Antibody Expression Services

Experimental content	Deliveries	Period
Gene synthesis & vector construction	1. Recombinant antibody 2. Expression vectors 3. Cloning strain 4. Lab report	6-8 Weeks
Plasmid extraction
Cell Transfection & Expression of Antibodies
Antibody purification (SDS-PAGE)

█ Tek Biotech Services

Fragment Antibody Construction and Production Services

Fragment antibodies include Fab antibody, scFv and VHH antibody (camel-derived nanoantibodies), etc. Customers can directly provide Fab, scFv or VHH sequences to Tek Biotech for recombinant expression and obtain high purity products. If customers only have target antigen information, they can entrust Tek Biotech to conduct animal immunization and screen scFv, VHH and other antibodies.

Recombinant Antibody 293F/CHO Cell Expression Service

Full set of Gibco serum-free mammalian cell culture for scientists' needs of in vitro recombinant expression of natural conformational proteins, such as glycosylation modification, phosphorylation modification and so on. The full set of services provided to customers meets the GMP-like system, including cell seed bank source documentation record system, cell seed batch verification, quality control of animal source components, standardized cell culture and transformation operation procedures, full set of purification fillers and equipment provided by GE, and other guidelines for the production of recombinant proteins.

█ Service Advantages

-- Detailed experimental design and demonstration: including rare codon analysis, antibody sequence analysis, expression system selection, expression vector construction, antibody modification, etc.

-- Multiple labeled antibody expression: His-tag fusion expression, isotope labeling expression, biotin labeling expression.

-- Preparation of recombinant antibodies of multiple genera: human, mouse, rabbit, sheep, canine, camel, alpaca, bovine, etc.

-- Antibody modification control: multiple control of glycosylation and phosphorylation modifications.

-- Multiple expression modes: stable expression and transient expression

-- Complementary high expression vectors for lactation systems and amplification systems of various sizes.

-- Low endotoxin levels:<0.1EU/ug by LAL assay.

-- Complete documentation system to ensure traceability of all materials, reagents and preparation information for your products.

Recombinant Fragment Antibody Customization Service Frequently Asked Questions

Q: The expression level of recombinant fragment antibodies in the host system is low, resulting in 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 fusion tags or enhancers to improve the expression efficiency of antibodies.
Q: The structure or activity of recombinant fragment antibodies is affected, resulting in incomplete function or inability to express normally.

A: Optimize the structure of antibodies to ensure their correct folding and function; Evaluate the activity and stability of antibodies through structural prediction and analysis; Perform functional validation to confirm the activity and specificity of the antibody.
Q: The selected recombinant fragment antibody may not be suitable for specific research needs, affecting subsequent applications.

A: Select appropriate antibody fragments based on research objectives and needs, such as Fab fragments, scFv fragments, etc; Conduct preliminary screening and evaluation to select the most suitable antibody fragment; Consider using a combination of multiple antibody fragments to enhance the effectiveness and application range of antibodies.

Q: The expression level of recombinant fragment antibodies in the host system is low, resulting in 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 fusion tags or enhancers to improve the expression efficiency of antibodies.
Q: The structure or activity of recombinant fragment antibodies is affected, resulting in incomplete function or inability to express normally.

A: Optimize the structure of antibodies to ensure their correct folding and function; Evaluate the activity and stability of antibodies through structural prediction and analysis; Perform functional validation to confirm the activity and specificity of the antibody.
Q: The selected recombinant fragment antibody may not be suitable for specific research needs, affecting subsequent applications.

A: Select appropriate antibody fragments based on research objectives and needs, such as Fab fragments, scFv fragments, etc; Conduct preliminary screening and evaluation to select the most suitable antibody fragment; Consider using a combination of multiple antibody fragments to enhance the effectiveness and application range of antibodies.

Consult Now Recombinant Fragment Antibody Customization Service

Recombinant Antibody Expression Platform

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Recombinant Fragment Antibody Customization Service Frequently Asked Questions

Q: The expression level of recombinant fragment antibodies in the host system is low, resulting in insufficient production.

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

Q: The selected recombinant fragment antibody may not be suitable for specific research needs, affecting subsequent applications.

Q: The expression level of recombinant fragment antibodies in the host system is low, resulting in insufficient production.

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

Q: The selected recombinant fragment antibody may not be suitable for specific research needs, affecting subsequent applications.

Consult Now Recombinant Fragment Antibody Customization Service