Product Description
The OX101 monoclonal antibody reacts with CD47, an immunoglobulin superfamily protein that is ubiquitously expressed in various cells, including platelets and RBCs. CD47 is a heavily N-glycosylated multi-pass transmembrane protein with extracellular, helical, and cytoplasmic domains. This protein was originally identified as integrin-associated protein (IAP) and ovarian carcinoma antigen OA3, but subsequent studies identified CD47 as a marker of self on murine RBCs to prevent RBC clearance by splenic red pulp macrophages in the bloodstream by binding to SIRPalpha. CD47 binding partners include SIRPalpha, SIRPgamma, TSP1, VEGFR-2, Serpin A1, Integrins (alphav3, alphaM2, alpha41, etc.), BNIP3, CDC42, PI3K, Src, and others. CD47 functions as a cognate receptor for TSP1, and the CD47-TSP1 pathway plays a significant role in the pathophysiology of vascular disease, wherein CD47-TSP1 signaling acts via adenylate cyclase activation, stimulation of apoptosis, and regulation of nitric oxide and Nox1. Besides various normal cells, CD47 is also expressed in various tumor cells, and studies have established CD47 as a biomarker of malignant tumors. By blocking the CD47-SIRPalpha interaction in cancer cells, scientists have found that the CD47-SIRPalpha axis acts as a tumor phagocytosis checkpoint, telling macrophages dont eat me. This signaling is thought to be a way for many tumor cells to escape the immune system. The CD47-SIRPalpha signaling axis controls immunity through the Hedgehog/SMO/Gli1 signaling pathway, and the blockade of CD47 or targeting its binding protein SIRPalpha is known to upregulate both innate and adaptive anti-tumor immune responses. Targeting CD47 and its regulators is emerging as a promising therapeutic approach in cancer immunotherapy, and preclinical experiments have indicated CD47 blockade to demonstrate potent anti-cancer activity in several hematologic cancers.
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