The blood group B lectin present in the mushroom Marasmius oreades is highly specific for Galα1,3Gal and also recognizes the porcine xenotransplantation epitope Galα1,3Galß1,4GlcNAc/Glc and the blood group B determinant. Marasmium oreades agglutinin (MOA) is specific towards these epitopes present on chain ends of glycoproteins (e.g. porcine tissues and organs, bovine thyroglobulin, 3T3 cells, murine laminin, Ehrlich ascites tumor cells) and glycolipids. In vivo studies have shown glomerular microvascular endothelial binding of this lectin, thus this conjugate could be used as an effective tool for studying glomerular endothelial injury, acute kidney failure, and thrombotic microangiopathies.
MOA-SAP is a bonded conjugate between the blood group B lectin present in the mushroom Marasmius Oreades and the secondary conjugate Streptavidin-ZAP (IT-27) containing the ribosome-inactivating protein, saporin.
MOA-SAP eliminates cells expressing Galα1,3Gal and Galα1,3Galß1,4GlcNAc/Glc.
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