Cell surface associated a2,6-sialic acid is an important factor in the tumorgenicity and invasiveness of cancer cells, as well as the susceptibility to viral infection. a2,6-sialylytransferase overexpression results in increased cell surface a2,6-sialic acid and is correlated with cancer progression. This enzyme may be used to study sialylation of glycoproteins and the resulting effects on cellular recognition, adhesion, and signaling.

Product - Soluble, recombinant, human a 2,6-(N)-sialyltransferase, (lacking the N-terminal membrane spanning region) fused at the N-terminus to a His•Tag® sequence and expressed in S. frugiperda insect cells using a baculovirus expression system. Sialylates N-linked glycoprotein oligosaccharides. Exhibits strict specificity for the Galß1,4GlcNAc sequence of oligosaccharides transferring sialic acid to the 6-position of galactose.