Human Siglec-5/Siglec-14 Biotinylated Antibody

Siglecs (1) (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins (2) belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding (3), followed by varying numbers of Ig-like C2-type domains (1, 4). Eleven human Siglecs have been cloned and characterized (1, 4). They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and the Siglec-5 to 11 (4, 5,  6). To date, no Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Siglec-5 to 11 share a high degree of sequence similarity with CD33/Siglec-3 both in their extracellular and intracellular regions. They are collectively referred to as CD33-related Siglecs. One remarkable feature of the CD33-related Siglecs is their differential expression pattern within the hematopoietic system (4, 5). This fact, together with the presence of two conserved immunoreceptor tyrosine-based inhibition motifs (ITIMs) in their cytoplasma tails, suggests that CD33-related Siglecs are involved in the regulation of cellular activation within the immune system.