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The specificity and binding affinity of sar408701 to human and cynomolgus monkey ceacam5 were tested in vitro. To achieve this, we performed biopanning in our library and obtained an antibody candidate, b9, which bound potently and specifically to ceacam5 protein and possessed excellent biophysical. These results suggested that the amides of residues 627 and 628 are not involved in the ceacam5 epitope
We performed biopanning in our library and obtained an antibody candidate b9, which bound potently and specifically to ceacam5 protein (k d = 4.84 nm) and possessed excellent biophysical properties (low aggregation tendency, high homogeneity, and thermal stability).
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