Recombinant Human ST6GALNAC2 protein is a Human Full Length protein, in the 1 to 374 aa range, expressed in Wheat germ and suitable for ELISA, WB.
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Application | Reactivity | Dilution info | Notes |
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins (PubMed:10742600, PubMed:29251719). Shows a preference for N-acetylgalactosamine (GalNAc) residues already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage (PubMed:10742600).
SIAT7B, SIATL1, STHM, ST6GALNAC2, ST6GalNAc II, SThM, Sialyltransferase 7B, ST6GalNAcII, SIAT7-B
Recombinant Human ST6GALNAC2 protein is a Human Full Length protein, in the 1 to 374 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins (PubMed:10742600, PubMed:29251719). Shows a preference for N-acetylgalactosamine (GalNAc) residues already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage (PubMed:10742600).
Belongs to the glycosyltransferase 29 family.
ST6GALNAC2 also known as GalNAc α-26-sialyltransferase 2 is an enzyme involved in the sialylation process. Its molecular mass is approximately 56 kDa. The enzyme is expressed prominently in human tissues like the colon small intestine and spleen. ST6GALNAC2 catalyzes the transfer of sialic acid from CMP-NeuAc to GalNAc residues of glycoproteins and glycolipids playing a role in modifying their structures.
The enzyme has a significant role in the biosynthesis of sialylated structures influencing cell-cell interactions signaling and immune modulation. ST6GALNAC2 is part of the glycosyltransferase family and it acts without forming larger complexes. Its activity affects the surface glycosylation pattern of cells influencing properties like cell adhesion and signaling pathways that are critical for cellular communication.
Sialylation influences cellular interactions and immune responses and ST6GALNAC2's addition of sialic acid units impacts these processes. It participates in the glycosphingolipid biosynthesis pathway and influences the sialylation branch of the Nglycosylation pathway. ST6GALNAC2's activities interplay with other sialyltransferases in regulating the sialylation state of glycoproteins affecting interactions with receptors such as selectins and integrins which are important in mediating cellular adhesion and trafficking.
Altered ST6GALNAC2 activity links to colorectal cancer and inflammatory bowel diseases. In colorectal cancer modifications in glycosylation patterns influenced by ST6GALNAC2 and related enzymes like ST6GALNAC1 correlate with tumor progression and metastasis. In inflammatory bowel diseases the enzyme contributes to changes in the mucosal barrier affecting immune responses and tissue integrity. Understanding ST6GALNAC2's role offers insights into therapeutic targets in these diseases.
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ab161069 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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