CDCP1 (CUB domain-containing protein 1), also known as CD318 or TRASK, is a transmembrane glycoprotein implicated in cancer progression and metastasis. Structurally, it contains three extracellular CUB domains, a transmembrane region, and intracellular tyrosine phosphorylation sites. Initially identified as a substrate of Src-family kinases, CDCP1 regulates cellular adhesion, migration, and signaling pathways linked to tumorigenesis.
Overexpression of CDCP1 is observed in various cancers, including lung, breast, and colorectal carcinomas, where it promotes invasive behavior and metastasis by modulating integrin-mediated signaling, epithelial-mesenchymal transition (EMT), and interactions with extracellular matrix components. Its intracellular domain interacts with proteins such as PKCδ and Src, influencing cell survival and metastatic dissemination.
CDCP1-targeting antibodies are primarily used as research tools to investigate its biological roles and as potential therapeutic agents. These antibodies enable detection of CDCP1 expression in tissues or cell lines via techniques like Western blotting, immunohistochemistry, and flow cytometry. Therapeutically, anti-CDCP1 antibodies are explored in preclinical models for their ability to block pro-metastatic signaling or deliver cytotoxic payloads via antibody-drug conjugates (ADCs). Despite promising results in reducing metastasis in animal studies, clinical translation remains in early stages, with challenges including optimizing specificity and understanding resistance mechanisms.
Overall, CDCP1 antibodies represent both a valuable research reagent and a potential avenue for targeted cancer therapy.