Biolegend, 569506, Biotinylated Recombinant Human CD47-Fc Chimera (carrier-free)

CD47 (Cluster of differentiation 47), also known as integrin-associated protein (IAP), is a ~50 kD glycosylated protein belonging to the immunoglobulin superfamily. It is a ubiquitously expressed integral membrane protein with a single IgV-like domain at its N-terminus, five membrane-spanning regions, and an alternatively spliced cytoplasmic C-terminus. CD47 was first identified as a protein involved in β3 integrin-mediated signaling in leukocytes. CD47 interacts with SIRPα (signal regulatory protein-alpha), TSP-1 (thrombospondin-1) and other integrin members to regulate cell migration, axon extension, cytokine production and T cell activation. CD47 binds to SIRP family members on macrophages, neutrophils and T cells. These interactions function as a negative immune checkpoint to prevent the macrophage-mediated clearance of healthy CD47-expressing cells. CD47 is a potent ‘do not eat me’ signal that enables cancer cells to evade detection by the innate immune system. Atherogenesis is associated with upregulation of CD47, a key antiphagocytic molecule that is known to render malignant cells resistant to programmed cell death. In several preclinical studies, therapeutic antibodies that block the interaction between CD47 and SIRPα promote effective antitumor responses by enabling elimination of both hematologic and solid tumor cells by phagocytes, enhancing cross-presentation of CD8 + T cells by antigen-presenting cells, and triggering adaptive immune responses.