Articles tagged with Antigen Binding Fragments
Researchers discover tiny antibody-like proteins from camels and llamas that can treat brain disorders like schizophrenia and Alzheimer’s disease with fewer side effects. The nanobodies are smaller than conventional antibodies, making them easier to produce and purify.
Researchers at UMC Utrecht discovered that converting monoclonal antibodies from IgG to IgM isotype can significantly broaden their ability to recognize and bind multiple human-relevant bacterial pathogens. This finding could guide the future design of antibody therapies against bacterial infections.
Researchers developed a high-volume method to rapidly build and test large numbers of antibodies at once, accelerating antibody research and treatment development. The oPool+ display platform has potential applications in influenza vaccination research, infectious disease treatment, and cancer research.
Scientists have engineered a monoclonal antibody that protects mice from a lethal dose of influenza A with sticky staying power. The new molecule combines specificity and broad binding capacity, adhering to the lung lining and blocking infection in mice.
Researchers have provided new details on structures resulting from 3D domain swapping in antibody light chains, shedding light on mechanisms of protein aggregation. The study suggests that the formation of tetramers may prevent protein aggregation by decreasing flexibility.
Scientists have identified a new class of 'bivalent' antibodies that can bind to two viral targets at once, neutralizing multiple Omicron variants. These potent antibodies retain efficacy against early SARS-CoV-2 variants and several later Omicron sub-lineages.
Researchers developed a Quenchbody fluorescent immunosensor that detects SARS-CoV-2 with exceptional speed and sensitivity. Adding a crowding agent enhances performance, allowing for lower detection limits and faster results. The technology shows promise for rapid and cost-efficient diagnosis of COVID-19 and other infectious diseases.