ST6GALNAC2
ST6GALNAC2 (ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 2, also known as ST6GalNAII, STHM, SIAT7, SIAT7B and SIATL1) is a Golgi sialyltransferase. It transfers sialic acid onto O-linked GalNAc glycan chains on glycoproteins. Browse Assay Genie's current range of ST6GALNAC2 research reagents below, or read on for the biology behind the target.
ST6GALNAC2 catalyses the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins. Specifically, it conjugates sialic acid through an alpha-2,6 linkage to N-acetylgalactosamine (GalNAc) chains attached to serine or threonine residues. Its substrates include alphaGalNAc- and Galbeta1-3GalNAc-O-Ser/Thr epitopes, better known as the Tn and T antigens, so the enzyme acts directly on core O-glycan structures.
The ST6GALNAC2 gene encodes a type of sialyltransferase that belongs to the glycosyltransferase 29 family and is classified by HGNC in the sialyltransferase gene group. The protein is a membrane-associated enzyme located in the Golgi apparatus, where glycan modification takes place. Researchers studying the ST6GALNAC2 protein often work with the mouse ortholog, St6galnac2.
Sialyltransferases add sialic acids to the nonreducing ends of glycoconjugates. According to the NCBI Gene summary, at the cell surface these modifications have roles in cell-cell and cell-substrate interactions, bacterial adhesion and protein targeting. The gene has carried several names over time, including sialyltransferase 7, sialyltransferase-like 1 and ST6 GalNAc alpha-2,6-sialyltransferase 2, which explains the aliases SIAT7, SIAT7B, SIATL1 and STHM that appear in the literature.
ST6GALNAC2 sialylates GalNAc-linked O-glycan chains on serine and threonine, making it a useful enzyme for studying O-linked glycoprotein modification.
The enzyme sialylates the Tn and T antigen epitopes, so it is relevant to work on how these glycan structures are modified.
Sialic acid modifications influence cell-cell and cell-substrate interactions, placing ST6GALNAC2 in studies of cell surface glycan function.
As a Golgi membrane sialyltransferase of the glycosyltransferase 29 family, it supports comparative study of glycan-processing enzymes.
ST6GALNAC2 transfers sialic acid in an alpha-2,6 linkage onto GalNAc glycan chains attached to serine or threonine in glycoproteins. It acts on alphaGalNAc- and Galbeta1-3GalNAc-O-Ser/Thr epitopes, also called the Tn and T antigens, and it resides in the Golgi apparatus membrane.
Aliases and earlier symbols include ST6GalNAII, STHM, SIAT7, SIAT7B and SIATL1. Previous names include sialyltransferase 7, sialyltransferase-like 1 and ST6 GalNAc alpha-2,6-sialyltransferase 2. Check these synonyms when searching literature, as older papers may use them instead of the current symbol.
A mouse ortholog, St6galnac2, is recorded for this gene. The enzyme belongs to the glycosyltransferase 29 family of sialyltransferases. If you plan work in a particular species, check the datasheet of any product for its validated reactivity.
Other sialyltransferases and related targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9UJ37; product specifications from Assay Genie datasheets.