Mouse Anti-Human CD93 Antibody (S-4392)

CD93 is a highly glycosylated type I transmembrane protein encoded by the C1QR1 gene (also known as CDw93 or ECSM3) on chromosome 20p11.21. Its extracellular region comprises a C-type lectin-like domain (CTLD), five epidermal growth factor (EGF)-like domains, and a mucin domain. Initially misidentified as a receptor for complement C1q, CD93 is now understood to primarily interact with Moesin via its intracellular tail to mediate cytoskeletal remodeling. On endothelial cells, it binds ligands such as multimerin-2 (MMRN2) or insulin-like growth factor binding protein 7 (IGFBP7) to activate the β1 integrin/FAK signaling axis, thereby promoting fibronectin fibrillogenesis and filopodia formation—processes that drive tumor angiogenesis and vascular maturation. Furthermore, CD93 exerts dual immunomodulatory functions on monocytes and macrophages. On one hand, its extracellular CTLD can directly bind bacterial CpG DNA and present it to Toll-like receptor 9 (TLR9), exacerbating inflammatory responses. On the other hand, in hepatocellular carcinoma, glycolysis-induced upregulation of CD93 on monocytes enhances PD-L1 expression via the AKT-GSK3β axis and induces secretion of the extracellular matrix component Versican, collectively suppressing CD8⁺ T cell activation and intratumoral infiltration. Blocking CD93 with therapeutic monoclonal antibodies has been shown to normalize tumor vasculature by upregulating adhesion molecules (ICAM1/VCAM1), significantly improving the infiltration efficiency of adoptive T cell therapies in solid tumors. Simultaneously, specific blockade of CD93 on monocytes can reverse the immunosuppressive microenvironment. These attributes position CD93 as a next-generation pan-cancer therapeutic target capable of simultaneously modulating angiogenesis and adaptive immune tolerance.