Clone REA393 recognizes the human siglec-5 and siglec-14 antigens, which are both single pass transmembrane protein members of the immunoglobulin superfamily. Siglec-5 is also known as CD170. Siglec-5 has four extracellular Ig-like domains and a cytosolic inhibitory motif. Siglec-14 was discovered with three Ig-like domains and has almost complete sequence identity with siglec-5 at the first two Ig-like domains, shows a glycan binding preference similar to that of siglec-5, and associates with the activating adapter protein DAP12. Siglec-5 is expressed on granulocytes and monocytes as well as on plasmacytoid dendritic cells, monocyte-derived dendritic cells, and macrophages. It is potentially involved in the negative regulation of innate immune responses, and also suggested to be a useful diagnostic and therapeutic marker for acute myelogenous leukemia. Siglec-14 is expressed on granulocytes and B cells. Some individuals lack the expression of siglec-14, while they all express siglec-5.

Additional information: Clone REA393 displays negligible binding to Fc receptors.