Glycoproteins in human tumors often exhibit abnormal glycosylation patters, e.g. certain Lewis structures, TF antigen, Tn antigen and/or their sialylated forms, which creates additional binding sites for glycoreceptors. The C-type lectin domain family 10 member A (CLEC10A/MGL/CD301) is a calcium-type (C-type) lectin glycoreceptor expressed on dendritic cells (DCs) (Suzuki et al. 1996). It recognizes glycoproteins from both altered self and pathogens due to its monosaccharide specificity for galactose (Gal) and N-acetylgalactosamine (GalNAc). CLEC10A specifically binds glycans with terminal GalNAc residues such as Tn antigen (GalNAcalpha-serine/threonine), 6-sulfo-Tn, Lac-di-NAc (Galbeta1,4-GlcNAc) as well as core 5 (GalNAcalpha1-3GalNAcalpha-) and core 6 (GlcNAcbeta1-6GalNAcalpha-) that are expressed in human tumors (Mortezai et al. 2013, van Vliet et al. 2005). CLEC10A on immature human monocyte-derived DCs has been shown to recognize and internalize the three tandem repeat peptides of Mucin-1 carrying Tn (Tn-MUC1) (Denda-Nagai et al. 2010).