Marasmius oreades agglutinin (MOA) derives from the Marasmius oreades mushroom. MOA consists of an intact 33 kDa and truncated 23 kDa subunit as well as a 10 kDa polypeptide. MOA has been used to study glomerular endothelial injury and to agglutinate B-type red blood cells.
This recombinant protein binds specifically to blood group B antigens and has a high affinity to alpha-Gal, a carbohydrate found on B-type blood cells. Recombinant MOA was expressed in E. coli and purified using affinity chromatography. It has been conjugated to biotin via an amide bond. This product is routinely tested by coomassie stain of a SDS-PAGE gel and agglutination assay.
Applications include red blood cell (RBC) agglutination.
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