Siglec-10 is a lectin that specifically binds alpha-2,3- or alpha-2,6-linked sialic acid. It is a member of the Ig-superfamily and is expressed in monocytes, eosinophils, B cells, and a subset of NK cells. Siglec-10 is a single pass transmembrane protein. The extracellular domain contains one V-set Ig-like domain and three C2-set domains; the cytoplasmic domain contains one immunoreceptor tyrosine-based inhibitor motif (ITIM) which, after tyrosine-phosphorylation, recruits SH2-family phosphatases such as SHP-1 and PTPN6, resulting in the blocking of the signal transduction. CD24 and the vascular adhesion protein-1 (VAP-1) have been described as ligands of Siglec-10.