Recombinant Mouse ST6GALNAC2 Protein, CF
Recombinant Mouse ST6GALNAC2 Protein, CF Summary
Ser28-Arg373, with a C-terminal 6‑His tag
Background: ST6 Sialyltransferase 2/ST6GALNAC2
Sialic acid molecules attached to glycoproteins or glycosphingolipids play important roles in various biological processes such as immune recognition, pathogen infection, and cell adhesion. Sialyltransferases are key enzymes that regulate the serum levels of sialic acid‑containing molecules. Alpha‑N‑acetylgalactosaminide alpha ‑2,6‑sialyltransferase 2, encoded by the ST6GALNAC2 gene, is a type II membrane protein localized in the Golgi network and catalyzes 2,6‑sialylation of the Tn antigen (GalNAc‑O‑Ser/Thr) (1). Sialyl‑Tn antigen is highly expressed in several human carcinomas and is associated with carcinoma aggressiveness and poor prognosis. Cells transfected with ST6GALNAC2 synthesized the sialyl‑6T structure [Gal beta 1‑3 (Neu5Ac alpha 2‑6)GalNAc‑O‑Ser/Thr] (2). In vitro analysis revealed that the enzyme can use both Gal beta 1‑3GalNAc and Neu5Ac alpha 2‑3Gal beta 1-3GalNAc as acceptor substrates (3). Recently, it has been reported that disregulation of this gene is involved in the pathogenesis of IgA nephropathy, a common kidney disease that occurs when antibody IgA accumulates in kidneys (4). The enzyme may also be used to synthesize a cancer vaccine (5, 6). At the protein level, mouse ST6GALNAC2 shows 75% amino acid sequence identity with the human homologue. The activity of this enzyme has been measured using a phosphatase‑coupled assay (7).
- Kono, M., et al. (2000) Biochem. Biophys. Res. Commun. 272:94.
- Marcos, N.T., et al. (2004) Cancer Res. 64:7050.
- Samyn-Petit, B., et al. (2000) Biochim. Biophys. Acta 1474:201.
- Li, G.S., et al. (2007) Hum. Mutat. 28:950.
- Julien, S., et al. (2009) Br. J. Cancer 100:1746.
- Sewell, R., et al. (2006) J. Biol. Chem. 281:3586.
- Wu, Z.L., et al. (2011) Glycobiology 21:727.
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