They have a high level of specificity reducing the risk of off-target side effects, and due to being fully human, reduces the risk of immunogenicity seen with non-human antibodies. Two fully human antibodies, 17-Fab and 3G12-Fab have been discovered. The use of antibodies specifically targeting ENPP1 could stimulate an immune response causing immunosuppression in the tumor leading to cell death.
One antibody, with a well-defined epitope and affinity in the nanomolar range, exhibited specific binding of CEACAM5 without any cross-reactivity to either membrane-distal domains of CECAM5 or >5,800 human surface proteins, suggesting the highest specificity of any reported CEACAM5 antibodies. However, developed anti-CEACAM5 antibodies for other cancers showed disappointing clinical results due to a lack of specificity and wrong epitope selection. Since existing CEACAM5 antibodies lack specificity and have unclear epitopes, making them poor candidates for cancer therapy, Pitt inventors identified the first fully human monoclonal antibodies binding to membraneproximal domain of CEACAM5 from large phage display libraries.
While current tools rely primarily on polyclonal antibodies or a single monoclonal antibody to nsP2, this technology introduces two distinct antibodies per nsP, significantly enhancing detection accuracy. This technology employs a set of mouse-derived monoclonal antibodies tailored to recognize each of the four chikungunya virus nonstructural proteins (nsPs). Designed for applications such as Western blot, immunoprecipitation, and immunofluorescence, these highly specific antibodies enable researchers to analyze individual roles within the viral replicase complex.