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Recombinant Antibodies

High Quality Antibodies Delivering Superior Results

Antibody

Animal-Free, Highly Reproducible and Reliable

Recombinant antibodies (rAbs) offer numerous advantages over hybridoma-produced antibodies. rAbs are created in vitro using synthetic genes and can therefore be produced animal-free. There is no reliance on maintaining a stable hybridoma cell population and may reduce the risk of unwanted, non-specific binding. rAbs are highly reproducible with increased lot-to-lot consistency as the nucleic acid sequence is well-defined and can be exactly replicated. They can deliver more reliable binding than traditional antibodies and can be easily produced in large volume over a shorter time period. These highly specific and sensitive antibodies can be used in a wide range of applications.


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Recombinant Antibodies (rAb)
 

The Advantages of Recombinant Antibodies

High degree of lot-to-lot consistency and reproducibility
Improved sensitivity and specificity
Animal-free antibody production
Ease of scalability thus available in bulk
Custom formulations upon request

Recombinant Antibody Search

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What are Recombinant Antibodies?

What are the Various Types of Recombinant Antibody Fragments?

Fv, variable fragment –
The Fv fragment is the smallest antibody fragment that retains antigen binding capacity.
It consists of variable fragments of light (VL) and heavy (VH) chains, each of which is stabilized by an intramolecular disulfide bond. However, contacts between VH and VL involve only ionic interactions and therefore the structure of this fragment is very unstable. Structural stability of Fv fragments can be achieved by insertion of interchain disulfide bond.


scFv, single chain Fv in which light and heavy chain fragments are connected by a polypeptide linker –
The linker technology was a key step of success of constructing scfv antibody library. Scfvs have been developed as possible drug candidates in their own right, as well as components or domains of drug candidates. The scFv fragments are the “simplest” target for cloning and expression. However, they frequently exhibit lower stability and, sometimes, lower affinity; during therapeutic use, they are characterized by shorter half- lifetime in blood circulation compared with larger fragments.


(scFv)2, fragment that consists of two scFv molecules connected by a disulfide bond – The (scFv)2 fragments obtained by disulfide bond linking between C-terminal cysteine residues demonstrate better in vivo transport into tissues compared with the scFv-fragments during their use as therapeutic agents.

dsFv, variable fragment stabilized by additional intramolecular disulfide bond –
The bacterial and yeast expression systems are used for expression of small nonglycosylated antibody fragments dsFv.


Fab- and (Fab)2, fragments –
These are identical in their structure with fragments formed during proteolysis of full-length IgG anti- bodies by papain and pepsin, respectively.


VH, heavy chain variable domain –
Single-chain fragment variable (scfv) molecules combine the coding sequence of the variable heavy (VH) and sequence of the variable light chain (VL) domains of an antibody in a single-gene encoded format.


There are antibody derivatives known as “diabodies”, “triabodies”, and “tetrabodies” –
Their molecules consist of two, three, or four identical or different fragments of antibodies of the same or different specificity linked together.


A Single domain antibody (sdAb) was discovered in both camelids and nurse sharks that consist of a lone VH domain, lacking a paired VL, attached to a constant region. The primary advantages of domain antibodies as compared with scFvs are generally better folding and stability characteristics.

 

Learn more about Recombinant Antibodies

Read our TechNote: What are Recombinant Antibodies?

Worry-Free Antibody Trial Program

Are you ready to be Worry-Free?

Our Worry-Free Antibody Trial Program allows you to evaluate any of our antibodies of interest for any new application or species not currently listed on our datasheet without risk.

 

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