CDCP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 646 amino acids (30-667a.a.) and having a molecular mass of 72.8kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). CDCP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
CUB Domain Containing Protein 1 (CDCP1), also known as CD318, SIMA135, and TRASK, is a type I transmembrane glycoprotein. It is characterized by the presence of CUB domains, which are involved in protein-protein interactions. CDCP1 is predominantly located on the cell surface and plays a crucial role in various cellular processes, including cell adhesion, migration, and survival.
CDCP1 is composed of three extracellular CUB domains, a single transmembrane domain, and a short cytoplasmic tail. The CUB domains facilitate interactions with other proteins, while the cytoplasmic tail is involved in intracellular signaling. CDCP1 is known to interact with several key signaling molecules, including SRC family kinases and protein kinase C delta (PKCδ), which are involved in oncogenic signaling pathways .
CDCP1 is upregulated in a variety of malignancies, including cancers of the breast, lung, colorectum, ovary, kidney, liver, pancreas, and hematopoietic system . Elevated levels of CDCP1 are associated with progressive disease and poorer survival outcomes. It is implicated in several oncogenic processes, such as:
Given its significant role in cancer progression, CDCP1 has emerged as a potential biomarker and therapeutic target. Researchers are exploring various strategies to target CDCP1 for cancer diagnosis and treatment. For instance, radioligand therapy (RLT) targeting CDCP1 has shown promise in treating metastatic castration-resistant prostate cancer (mCRPC), including subsets with low prostate-specific membrane antigen (PSMA) expression .