n-CoDeR®

- Evolution Beyond Nature

The n-CoDeR® antibody library contains 30 billion functional human antibody genes (genes with open reading frame). All the antibodies have the same framework structure, which has low immunogenicity. However, the antibodies have different combinations of Complementarity Determining Regions (CDRs), which define the antigen binding specificity. These CDRs were originally isolated from the antibody genes of a large number of healthy volunteers. Using the n-CoDeR® technology the fully human CDRs are recombined into new antibody molecules. The unique recombination process allows the library to contain a wider variety of antibodies than could have been created naturally by the human immune system. This means that there is a higher likelihood of finding antibodies with high affinity and high specificity against a particular target.

Two library formats exist, one containing the smaller scFv antibody fragment and the other containing the Fab antibody fragment. Antibodies from the library are selected using an established technology called phage display. Selected targets are used as bait to fish out those antibodies that bind to the target. As n-CoDeR® is an in vitro system, the bait can take any format including cells, proteins or peptides. The relevant antibody genes can then be produced within E. coli bacteria.

We have developed an integrated robotics platform for the rapid selection, screening and identification of human antibodies from our n-CoDeR® library. The Robo-CoDeR™ platform has the capacity to screen more than twenty thousand antibody clones each day. Antibodies isolated from n-CoDeR® have shown affinities in the sub-nanomolar range against haptens, peptides, carbohydrates and proteins.

We currently use three active libraries, n-CoDeR®-scFv, n-CoDeR®-Fab-Lambda and n-CoDeR®-Fab-Kappa.

The n-CoDeR® library is protected by patents and patent applications in all markets of commercial interest.