Human ST6 Gal Sialyltransferase 1/ST6GAL1 Biotinylated Antibody

Sialic acid molecules attached to glycoproteins or glycosphingolipids play important roles in various biological processes such as immune recognition, pathogen infection, and cell adhesion (1). Sialyltransferases are key enzymes that regulate the cellular levels of sialic acid-containing molecules. Beta-galactosamide alpha‑2,6‑sialyltransferase 1 encoded by the ST6GAL1 gene is a type-II membrane protein localized in the trans-Golgi network and catalyzes 2,6-sialylation of Gal beta 1,4‑GlcNAc structures on N-glycans (2). The enzyme is involved in the generation of the cell-surface carbohydrate determinants and differentiation antigens HB‑6, CD75, and CD76 (3). ST6GAL1 is highly expressed in the liver and also expressed in most other tissues to some extent (4). ST6GAL1 deficiency causes abnormalities in B-cell immunoreactivity (5). The expression and activity of ST6GAL1 are associated with tumor metastasis in breast (6) and colon (7) cancers. The majority of ST6GAL1 in the liver is cleaved and secreted into the serum (8) and may be used as a biomarker for hepatitis diseases (9).