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DNA encoding the signal peptide and extracellular domain of human Siglec-3 (aa 1-259) chain was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.

Siglecs (or sialic acid-binding immunoglobulin superfamily lectins) are sialic acid-binding Ig-like lectins characterized by a homologous N-terminal V-set Ig-like domain and varying numbers of C2-set Ig-like domains. In humans 11 Siglecs have been described. Siglec-3 (CD33) is the smallest Siglec, with only 2 of these C2-set Ig domains. Siglec-3 is a 67 kDa glycoprotein found predominantly on myeloid cells, including early myeloid precursors in the bone marrow and certain subsets of mature circulating myeloid cells. Siglec-3 has also been reported on dendritic cells, cord blood-derived natural killer (NK) cells, in vitro expanded T cells, and some biphenotypic leukemias. Siglec-3 was initially described as a marker for normal and leukemic myeloid progenitor cells, but has received renewed interest due to its demonstrated lectin activity for alpha 2-6 and alpha 2-3 sialylated N-linked oligosaccharides expressed on red blood cells (RBCs) and certain myeloid cells. For a recent review on Siglecs please refer to Varki et al. (2006) Glycobiology 16:1R-27R.