Why Recombinant Antibodies?
Enhanced reproducibility and consistency
Recombinant antibodies are made from defined amino acid sequences and produced in a defined and reproducible manner. Traditional hybridoma production suffers from gene instability and cell-line drift which results in unknown antibody compositions. A published report revealed that more than 30% of 185 randomly selected hybridomas weren’t even truly monoclonal as they contained additional productive antibody heavy or light chains outside of their primary specificities. Recombinant antibodies eliminate all of these sources of lot-to-lot variability ensuring that future batches will be identical to previous batches.
Multiple format engineering
Recombinant antibodies can be reformatted into multiple variants thus allowing increased utility and options to the researcher. Traditional hybridomas can only be produced in their original format which may not be compatible with the desired utility. Our antibodies can be engineered with a variety of options including:
- Fc domains with different species or isotypes
- Molecularly defined antibody fragments and scaffolds such as Fabs and bispecifics
- Site-specific modifications such as defined biotinylation rather than unknown random biotinylation
- NullFc™ specific point mutations to drastically reduce Fc receptor interactions and reduce non-specific background binding
Highly defined expression
Our antibodies are produced via transient transfections of mammalian cell lines in a chemically defined, serum-free expression system which eliminates serum contamination and results in low endotoxin levels and highly pure antibodies.
The problem is that there are too many antibodies out there that are either non-specific (detect other targets in addition to – or in lieu of – the intended target), or not fit-for-purpose (not sensitive enough to detect endogenous signal or don’t work in the intended applications).