Recombinant Human ST6GALNAC6 protein is a Human Full Length protein, in the 1 to 333 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 - |
Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid with an alpha-2,3-linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b (PubMed:12668675, PubMed:17123352). Besides GMb1, MSGG and other glycolipids, it shows activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen (PubMed:12668675). Also has activity toward GD1a and GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) (By similarity).
SIAT7F, UNQ708/PRO1359, ST6GALNAC6, ST6GalNAc VI, Sialyltransferase 7F, ST6GalNAcVI, hST6GalNAc VI, SIAT7-F
Recombinant Human ST6GALNAC6 protein is a Human Full Length protein, in the 1 to 333 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid with an alpha-2,3-linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b (PubMed:12668675, PubMed:17123352). Besides GMb1, MSGG and other glycolipids, it shows activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen (PubMed:12668675). Also has activity toward GD1a and GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) (By similarity).
Belongs to the glycosyltransferase 29 family.
ST6GALNAC6 also known as ST6 N-acetylgalactosaminide alpha-26-sialyltransferase 6 is an enzyme with an important role in glycosylation processes. It has a molecular mass of about 59 kDa. The enzyme catalyzes the addition of sialic acid to glycoproteins and glycolipids specifically attaching to N-acetylgalactosamine-containing substrates. ST6GALNAC6 is expressed mainly in tissues such as the brain liver and digestive tract where it influences various physiological and biochemical modifications of cellular surfaces.
ST6GALNAC6 mods glycan structures and affects signal transduction and cell-to-cell interactions. It functions as a part of the sialyltransferase enzyme family altering glycoproteins and glycolipids which impact molecular mechanisms including cellular adhesion and migration. These actions influence cell communication and pathogenesis processes; however it's not known to work as a component of a significant protein complex.
ST6GALNAC6 influences the glycoprotein biosynthesis process and the sialylation pathway. It modifies molecules involved in the synthesis and modification of O-linked glycans impacting several proteins for instance mucins due to its role in the sialylation of glycoproteins. The enzyme's activities intersect with pathways involving other key glycosylation enzymes such as ST6GAL1 indicating its integrated role in glycan biosynthesis and cellular signaling cascades.
ST6GALNAC6 contributes to the development of conditions like cancer and cardiovascular diseases. Its altered expression is linked with cancer-related mechanisms due to changes in cell adhesion and metastasis as sialylation impacts how cancer cells interact with their environments. Additionally researchers associate its dysregulation with cardiovascular pathologies through impacts on related proteins such as mucins highlighting its influence on the progression of these diseases.
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ab162319 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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