Antibody discovery has undergone a transformation with advances in single B cell screening technologies. Biointron’s AbDrop™ platform leverages droplet-based microfluidics to access the full complement of antibody diversity, particularly within the complementary-determining regions (CDRs). CDRs are critical for the unique specificity and binding strength of an antibody, as these regions directly interact with target antigens.
The Role of CDR Diversity in Antibody Efficacy
The efficacy of any antibody largely depends on the diversity within its CDRs, particularly in CDR3 of the heavy chain, which is a major determinant of antigen binding. Broad CDR diversity enables the antibody to recognize a wider range of epitopes with high specificity, a quality that is especially valuable in therapeutic contexts where precision targeting is essential.
AbDrop™ uses the natural diversity present within the immune system, tapping into millions of primary plasma B cells to capture a wide array of naturally mature CDR sequences. This approach results in antibodies that exhibit a variety of high-affinity, high-specificity binding profiles without requiring extensive optimization.
Related: What are CDRs?
Accelerating the Development Timeline
Rapid NGS Sequencing: Within a week, AbDrop™ sequences the immunoglobulin genes of selected B cells, enabling an in-depth analysis of the CDR diversity and allowing researchers to make swift, data-driven decisions about which candidates to prioritize.
Expedited Candidate Selection: Because CDRs are already optimized for binding, the candidate selection process is significantly faster. In contrast to traditional methods that may take months to yield viable candidates, AbDrop™ can deliver high-affinity antibodies in just two to three months.
Our High-throughput Fully Human Antibody Discovery Platform integrates Cyagen’s HUGO-Ab™ mice with Biointron’s AbDrop™ microdroplet-based single B cell screening. This powerful combination accelerates the discovery and development of fully human antibodies, reducing the time from target identification to therapeutic candidate to just three months. Learn more about the service here.
Antibody specificity refers to an antibody's ability to selectively bind to a unique epitope on a target antigen while avoiding interactions with unrelated antigens. This property arises from the highly specialized antigen-binding site located in the variable region of the antibody, which determines its unique binding characteristics.
Antibody affinity refers to the strength of the binding interaction between a single antigen epitope and the paratope (binding site) of an antibody. This interaction is a fundamental measure of how well an antibody recognizes its specific antigen target.
Recombinant antibodies are produced using genetic engineering techniques, unlike traditional antibody production, where the immune system generates antibodies without direct control over their sequence. By introducing genes encoding antibody fragments into host cells, such as bacteria or mammalian cells, recombinant antibodies can be expressed, purified, and deployed for applications including research, diagnostics, and therapeutics.
Recombinant antibody expression is a biotechnological process that involves engineering and producing antibodies outside their natural context using recombinant DNA technology.
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