DR5 (Death Receptor 5), also referred to TNFRSF10B (Tumor necrosis factor receptor superfamily member 10B), TRAILR2 (TRAIL receptor 2) or CD262, is a 47.9 kDa cell surface receptor containing an intracellular death domain. The protein encoded by this gene is localized at the chromosome 8p21.3 and belongs to the tumor necrosis factor (TNF)-receptor superfamily. DR5 can be activated by TNFSF10/TRAIL/APO-2L, a TNF-related apoptosis inducing ligand, and responsible for transducing the apoptosis signal. This receptor is associated with several diseases including squamous cell carcinoma, head and neck and diffuse infiltrative lymphocytosis syndrome. Currently, a monoclonal antibody targeting DR5 marker has been developed and is under clinical trials for patients who suffer from various cancer types. FAP (Fibroblast activation protein), previously known as F19 cell surface antigen, is a cell surface serine protease with an extracellular catalytic domain. This type II membrane protease belongs to a prolyl-cleaving peptidase family. It is an endopeptidase with weak dipeptidase activity and the physiological substrate of FAP is α2-antiplasmin (α2-AP). FAP is expressed at sites of tissue remodeling during embryonic development and selectively produced in the stromal fibroblasts related to epithelial cancer. And FAP just has low or undetectable expression in the resting fibroblasts of the normal tissue in adults. Diseases linked to FAP include infiltrative basal cell carcinoma, hemophagocytic lymphohistiocytosis, and so on. It is reported that FAP support the tumor growth and proliferation, which makes it a novel target for anticancer therapies.