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Cytotoxic T-lymphocyte-associated protein-4 (CTLA-4) is a critical negative immunomodulatory receptor that is normally expressed in activated T cells and noticeably, in many cancerous cells. Indeed, molecular detection of CTLA-4 protein is crucial in basic research. In this work, the extracellular domain of the human CTLA-4 (hCTLA-4) protein was cloned, expressed, and purified. Subsequently, this protein was used as an antigen for camel ( Camelus dromedarius ) immunization to obtain polyclonal camelid sera against this protein. Furthermore, we evaluated the benefits of applying camelid hyperimmune sera containing heavy-chain antibodies in different antibody-based techniques. Our results indicated that hCTLA-4 protein was successfully expressed in the prokaryotic system. The polyclonal antibody (pAb) that raised against recombinant hCTLA-4 protein was able to detect the CTLA-4 protein in antibody-based techniques, such as enzyme-linked immunosorbent assay, western blotting, flow cytometry and immunohistochemistry (IHC) staining. This study shows that, due to the advantages such as multi-epitope-binding ability, camelid pAbs are potent to efficiently apply for molecular detection of CTLA-4 receptors in fundamental antibody-based researches such as IHC.

monoclonal antibodies in immunodiagnosis and immunotherapy

Evaluation of Laboratory Application of Camelid Sera Containing Heavy-Chain Polyclonal Antibody Against Recombinant Cytotoxic T-Lymphocyte-Associated Protein-4