Antibodies are commonly used reagents in research, diagnostics and therapeutics. They are specialized proteins, evolved by immune cells to specifically recognize foreign particles (antigens) and bind with high affinity. These properties make antibodies valuable tools in biomedical research and clinical applications. Obtaining antibodies to a desired target (for example a protein made by a tumor cell or invading virus) allows investigators to identify, purify and track targets. However, two major issues have negatively impacted biomedical and research use of antibodies. First, the ability and cost to make quality antibodies against desired targets (such as those that detect a chemical modifi...
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Antibodies are commonly used reagents in research, diagnostics and therapeutics. They are specialized proteins, evolved by immune cells to specifically recognize foreign particles (antigens) and bind with high affinity. These properties make antibodies valuable tools in biomedical research and clinical applications. Obtaining antibodies to a desired target (for example a protein made by a tumor cell or invading virus) allows investigators to identify, purify and track targets. However, two major issues have negatively impacted biomedical and research use of antibodies. First, the ability and cost to make quality antibodies against desired targets (such as those that detect a chemical modification on a protein). The predominant method is the hybridoma technique, developed in the 1970s. It is slow, expensive, and low-throughput, with success uncertain until well into the project. A second major issue, is ill-defined or poor-quality antibody characteristics. The hybridoma technique end point is an immune cell tumor line. Tumor cells can change over time and so can the quality of the antibodies they make. Problems with antibodies are one of the major contributors to the reproducibility crisis and published estimates are that millions of research dollars are wasted annually on poor quality antibodies. To correct this deficiency, leaders in the field have called for antibodies to be DNA sequence defined and made through recombinant methods. However, custom recombinant antibody (recAb) production is not available in a cost-effect manner. The Recombinant Antibody Production Core (RAPC) will provide custom recAbs to Texas investigators in a high-throughput, fast and cost-effective manner. Our methodology is particularly suited for targets the hybridoma method has difficulty producing antibodies against. Lastly recAbs, unlike hybridoma antibodies, can be further engineered and we propose options to produce antibodies engineered with enhanced functions.
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