ST6GAL12

ST6GAL12 is a human gene that encodes a member of the ST6GAL family of alpha-2,6-sialyltransferases, enzymes that modify glycans by adding sialic acid in an alpha-2,6 linkage. Sialyltransferases in this family are typically type II transmembrane proteins localized to the Golgi apparatus, where they transfer sialic acid from the donor substrate CMP-Neu5Ac to galactose residues on N- and O-linked glycans, generating alpha-2,6-sialylated structures such as Neu5Acα2-6Galβ1-4GlcNAc.

The precise function of ST6GAL12 in humans is not well characterized. As with other family members, it is expected to influence glycan architecture on the cell surface, which can affect cell–cell and cell–matrix interactions, receptor activity, and immune recognition. However, detailed information on its enzymatic activity, substrate preferences, tissue distribution, and physiological roles has not been extensively described in the publicly available literature.

Genomic and research notes indicate that ST6GAL12 is listed in gene databases as part of the ST6GAL sialyltransferase subfamily, but current knowledge about its expression patterns across tissues or involvement in disease remains limited. Much of what is understood about the potential roles of ST6GAL12 is inferred from studies of related ST6GAL enzymes rather than from direct characterization of this specific gene. Further research is needed to define its exact biochemical activity and biological significance.