Description
Product Characteristics: ST3gal6 Antibody: Sialyltransferases catalyze the transfer of sialic acid from cytidine 5-prime monophospho-N-acetylneuraminic acid (CMP-NeuAc) to terminal positions of glycoprotein and glycolipid carbohydrate groups. Terminal NeuAc residues are key determinants of carbohydrate structures, such as the sialyl-Lewis X determinants, and are widely distributed in many cell types. However, cancer cells often express more heavily sialylated glycans on their cell surface and this feature sometimes correlates with invasiveness. In contrast, expression of ST3gal6, a member of the sialyltransferase family that sialylates type II lactosamine structures on glycoproteins and glycolipids, was found to be significantly decreased by hypermethylation of the gene in gastrointestinal cancer. At least three isoforms of ST3gal6 are known to exist.
Target Information: The protein encoded by this gene is a member of the sialyltransferase family. Members of this family are enzymes that transfer sialic acid from the activated cytidine 5'-monophospho-N-acetylneuraminic acid to terminal positions on sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins. This protein has high specificity for neolactotetraosylceramide and neolactohexaosylceramide as glycolipid substrates and may contribute to the formation of selectin ligands and sialyl Lewis X, a carbohydrate important for cell-to-cell recognition and a blood group antigen. Alternative splicing results in multiple transcript variants that encode different protein isoforms. [provided by RefSeq, Sep 2012]