CD47 mAb (B6H12.2), InVivoPure+

CD47 (also known as Integrin-Associated Protein, IAP) is a ubiquitously expressed transmembrane protein involved in immune evasion by sending a “don’t eat me” signal via its interaction with SIRPα on macrophages. It plays a critical role in tumor immune evasion, self-recognition, and apoptosis regulation. The B6H12.2 antibody is a mouse monoclonal that specifically binds to human CD47. It has been widely cited in both in vitro and in vivo studies, including for blockade of CD47–SIRPα signaling to enhance phagocytosis of tumor cells. In addition to its primary function, the anti-CD47 mAb blocks the association between CD47, TSP1 (Thrombospondin 1) and integrin ανβ3 that promotes vitronectin-associated spreading of melanoma cells. The antibody reacts with vitronectin receptors on human polymorphonuclear leukocytes (PMN, neutrophils) and effectively blocks the receptor binding to the tripeptide Arg-Gly- Asp (RGD). This inhibition extends to RGD-stimulated phagocytosis, demonstrating its functional versatility. Importantly, B6H12.2 does not react with gpIIb/III or the LFA-1/Mac-1 family of cellular adhesion receptors, ensuring targeted specificity. Widely used in immunological assays such as immunohistochemistry and flow cytometry, B6H12.2 is a reliable tool for researchers studying CD47-expressing cells.