Epitope mapping is a crucial step in the development of therapeutic antibodies, vaccines, and diagnostic markers. It is vital for antibody selection, IP protection, and regulatory approval.
Most epitopes are discontinuous, emerging not from a linear sequence but from the 3D-structure of the antigen. Traditional linear epitope mapping simply overlooks these complex forms.
We predict conformational and discontinuous epitope candidates with computational methods and structural insights.
The resulting tens of thousands of epitope candidates are synthesized on a high-density peptide microarray, forming a seamless transition from prediction to validation.
This integrated approach allows studying all linear and discontinuous epitopes within one experiment.
Deriving discontinuous and linear epitope candidates from UniProt, AlphaFold, and proprietary algorithms.
Closely mimicking natural conformations, critical for presenting native-like epitopes.
With up to 200,000 custom peptides per chip, covering all possible conformational epitopes of most antigens.
