A Monoclonal Antibody That Recognizes a 110-kDa Protein Primarily Located on the Platelet α-Granule, Which Is Translocated to and Upgraded on the Surface Membrane of Platelets upon Activation

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Abstract
A murine monoclonal antibody, designated as MAb AAP2, was produced by immunizing human activated platelets to BALB/c mice. MAb AAP2 recognizes a platelet membrane antigen that was present in trace amount on the membrane of resting platelets, and was strongly expressed on the membrane after activation with thrombin as demonstrated by immunofluorescence microscopy. Platelet granule fractionation by ultracentrifugation on sucrose density gradient and metrizamide showed that the target antigen of MAb AAP2 was located in α-granules but not in lysosomes or dense granules. On Western blot prepared with whole platelet lysate, MAb AAP2 bound to a 110-kDa protein under nonreducing and reducing conditions. These results suggest that MAb AAP2 recognizes a 110-kDa platelet antigen, which is primarily located on the α granule of platelets and translocated to and upgraded on the surface membrane upon activation.