Anti-TEM1 CD248 Antibody

Tumor endothelial marker (TEM) 1 was originally identified as a human embryonic fibroblast-specific antigen and was later determined to be endosialin, a single-pass transmembrane glycoprotein that has multiple extracellular domains, including three EGF-like domains, a sushi-like domain, and a C lectin-like domain. TEM proteins are significantly up-regulated during angiogenesis and neoangiogenesis that are crucial for the growth of solid tumors. While TEM1 is not required for angiogenesis during fetal development, postnatal growth or wound healing, it plays a role in tumor growth, invasion, and metastasis. Fibronectin and collagen types I and IV act as specific ligands of TEM1, leading to suggestions that these molecules may cause changes in the extracellular matrix, cell adhesion and migration during tumor invasion.

Anti-TEM-1 antibody was raised against a peptide corresponding to 14 amino acids near the carboxy terminus of human TEM-1. The immunogen is located within the last 50 amino acids of TEM-1.

Expressed in tumor endothelial cells but absent or barely detectable in normal endothelial cells. Expressed in metastatic lesions of the liver and during angiogenesis of corpus luteum formation and wound healing. Expressed in vascular endothelial cells of malignant tumors but not in normal blood vessels. Expressed in stromal fibroblasts.