Red blood cells, which were thought to be devoid of annexin A7, were recently shown to harbor the 47 kDa isoform together with its binding partner sorcin [7]. We showed the presence of the 51 kDa isoform as well, adding red blood cells to the list of cells that harbor this isoform. Salzer et al. [7] not only demonstrated the presence of annexin A7 in red blood cells, they also showed that annexin A7 and sorcin were enriched in membrane raft domains of nanovesicles formed from red blood cells in vitro. Raft domains in general are considered key players in membrane organization and in mediating the vesiculation process. They result from the clustering of sphingolipids and cholesterol in the outer leaflet of the membrane connected to phospholipids and cholesterol in the inner leaflet and are enriched in special proteins. Biochemically rafts are defined as membranes that are resistant to extraction by cold Triton X-100 and can be floated to low densities in sucrose gradient centrifugation [36].