Anti-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.

ST3gal6 antibody was raised against a 16 amino acid synthetic peptide from near the carboxy terminus of human ST3gal6. The immunogen is located within amino acids 230 - 280 of ST3gal6.

Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3- sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1.

ST3gal6 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.