Fully Human Antibody Library
We have constructed a human full length IgG library (BioAtla HuAb-SD library) with large numbers of high diversity fully human antibodies expressed in mammalian cells. Using our proprietary bioinformatic analysis tools and rational design strategies, we have been able to maximize the combinatorial diversity of human immunoglobulin heavy and light chains in our library and have complete control over amino acid composition of the library. As a result, we are able to minimize the creation of undesired amino acids in the antibodies, while at the same time, creating antibodies with the highest affinities.
We have optimized our high throughput screening and validation process to increase the likelihood of identifying human antibodies with correct epitope recognition, high selectivity and the desired function. Further, we express our library in mammalian cells, bypassing many problems encountered with many of the traditional techniques used in antibody engineering. The issues associated with using phage, yeast and ribosomal display methods include lack of proper protein folding, posttranslational modifications, sub-optimal codon usage and finally inability to successfully transfer the antibody candidates into mammalian expression systems to produce therapeutic antibodies. Our fully human antibody library platform provides a mammalian cell environment for antibody selection and affinity maturation, coupled with a rapid, robust and simple screening process resulting in a process superior to other human antibody technologies.