Antibodies from hybridomas are not the only option when it comes to affinity reagents – there are many methods of generating binders. Some offer interesting structural options (e.g. single domain binders) or a functional advantage (e.g. binding to difficult non-peptide targets).
However, limitations prevent non-antibody binders from becoming widely adopted research reagents:
- There are few commercially available secondary reagents to detect binding and/or amplify signal
- Non-antibody binders have fewer conjugation sites
- Non-antibody binders often have a short in vivo half-life, and can have no effector function
Absolute Antibody is overcoming these limitations with recombinant technology, and making these reagents more accessible. An overview of the antibody formats featured on this page can be found here.
Case Study: From scFv to IgG
The scFv BG4 recognises G-Quadruplex (G4) nucleic acid structures, which are of interest in the study of genome function. As an scFv, BG4 requires a specialist secondary reagent and a tertiary reagent for visualisation. Absolute Antibody has engineered the BG4 binding domains onto common antibody backbones, making it compatible with the detection reagents already present in most labs.
Our engineered BG4 retains activity against both DNA and RNA G-quadruplex structures. Many thanks to the Balasubramanian Group at the University of Cambridge (who first generated the scFv) for providing ELISA data.
Case Study: From scFv to Long-Neck-scFv-Fc Fusion Protein
Trimethylated lysine residues on histone H3 are important epigenetic markers. Absolute Antibody offers two highly selective antibodies specific to two residues of interest – H3K4me3 and H3K9me3.
Case Study: Rabbit Anti-Mouse PD-L1 – Three Ways
Even if the original binder is unusual, our recombinant technology can make it compatible with standard protocols and secondary reagents. This figure highlights three binders – originally an scFv, camelid VHH, and rat IgG2a – performing in a rabbit IgG format.
Ab00840 Anti-PDL1 [VHH-PD-L1]*