Beta-galactoside alpha-2,6-sialyltransferase 1 is an enzyme that in humans is encoded by the ST6GAL1gene.[5]
The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein, which is normally found in the Golgi but which can be proteolytically processed to a soluble form, is involved in the generation of the cell-surface carbohydrate determinants and differentiation antigens HB-6, CDw75, and CD76. This protein is a member of glycosyltransferase family 29. Three transcript variants encoding two different isoforms have been found for this gene.[6]
Transcripts of ST6GAL1 are found in mouse high endothelial cells of mesenteric lymph node and Peyer's patches, and it could be involved in the B cell homing to Peyer's patches.[7]
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Rabouille C, Hui N, Hunte F, et al. (1995). "Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides". J. Cell Sci. 108. ( Pt 4) (4): 1617–27. doi:10.1242/jcs.108.4.1617. PMID7615680.
Lo NW, Lau JT (1996). "Novel heterogeneity exists in the 5'-untranslated region of the beta-galactoside alpha 2,6-sialytransferase mRNAs in the human B-lymphoblastoid cell line, louckes". Biochem. Biophys. Res. Commun. 228 (2): 380–5. doi:10.1006/bbrc.1996.1670. PMID8920923.