142 Results for: "Carbohydrates and Sugars"

Supplier: Bioss

Guanylyltransferase enzymes transfer one molecule of GTP to another molecule and also function in the transfer of guanosine nucleotides to sugar molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. L-fucose is an important sugar in complex carbohydrates that is frequently found on plant and mammalian N-linked glycans. FPGT (Fucose-1-phosphate guanylyltransferase), also known as GFPP (GDP-L-fucose pyrophosphorylase), is a 594 amino acid cytoplasmic protein that catalyzes the formation of GDP-L-fucose from L-fucose-1-phosphate and GTP. FPGT functions to reutilize the L-fucose that is produced uopn glycoprotein and glycolipid turnover.

Supplier: Bioss

Guanylyltransferase enzymes transfer one molecule of GTP to another molecule and also function in the transfer of guanosine nucleotides to sugar molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. L-fucose is an important sugar in complex carbohydrates that is frequently found on plant and mammalian N-linked glycans. FPGT (Fucose-1-phosphate guanylyltransferase), also known as GFPP (GDP-L-fucose pyrophosphorylase), is a 594 amino acid cytoplasmic protein that catalyzes the formation of GDP-L-fucose from L-fucose-1-phosphate and GTP. FPGT functions to reutilize the L-fucose that is produced uopn glycoprotein and glycolipid turnover.

Supplier: Bioss

Guanylyltransferase enzymes transfer one molecule of GTP to another molecule and also function in the transfer of guanosine nucleotides to sugar molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. L-fucose is an important sugar in complex carbohydrates that is frequently found on plant and mammalian N-linked glycans. FPGT (Fucose-1-phosphate guanylyltransferase), also known as GFPP (GDP-L-fucose pyrophosphorylase), is a 594 amino acid cytoplasmic protein that catalyzes the formation of GDP-L-fucose from L-fucose-1-phosphate and GTP. FPGT functions to reutilize the L-fucose that is produced uopn glycoprotein and glycolipid turnover.

Supplier: Bioss

Guanylyltransferase enzymes transfer one molecule of GTP to another molecule and also function in the transfer of guanosine nucleotides to sugar molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. L-fucose is an important sugar in complex carbohydrates that is frequently found on plant and mammalian N-linked glycans. FPGT (Fucose-1-phosphate guanylyltransferase), also known as GFPP (GDP-L-fucose pyrophosphorylase), is a 594 amino acid cytoplasmic protein that catalyzes the formation of GDP-L-fucose from L-fucose-1-phosphate and GTP. FPGT functions to reutilize the L-fucose that is produced uopn glycoprotein and glycolipid turnover.

Supplier: Bioss

Guanylyltransferase enzymes transfer one molecule of GTP to another molecule and also function in the transfer of guanosine nucleotides to sugar molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. L-fucose is an important sugar in complex carbohydrates that is frequently found on plant and mammalian N-linked glycans. FPGT (Fucose-1-phosphate guanylyltransferase), also known as GFPP (GDP-L-fucose pyrophosphorylase), is a 594 amino acid cytoplasmic protein that catalyzes the formation of GDP-L-fucose from L-fucose-1-phosphate and GTP. FPGT functions to reutilize the L-fucose that is produced uopn glycoprotein and glycolipid turnover.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Guanylyltransferase enzymes transfer one molecule of GTP to another molecule and also function in the transfer of guanosine nucleotides to sugar molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. L-fucose is an important sugar in complex carbohydrates that is frequently found on plant and mammalian N-linked glycans. FPGT (Fucose-1-phosphate guanylyltransferase), also known as GFPP (GDP-L-fucose pyrophosphorylase), is a 594 amino acid cytoplasmic protein that catalyzes the formation of GDP-L-fucose from L-fucose-1-phosphate and GTP. FPGT functions to reutilize the L-fucose that is produced uopn glycoprotein and glycolipid turnover.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Guanylyltransferase enzymes transfer one molecule of GTP to another molecule and also function in the transfer of guanosine nucleotides to sugar molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. L-fucose is an important sugar in complex carbohydrates that is frequently found on plant and mammalian N-linked glycans. FPGT (Fucose-1-phosphate guanylyltransferase), also known as GFPP (GDP-L-fucose pyrophosphorylase), is a 594 amino acid cytoplasmic protein that catalyzes the formation of GDP-L-fucose from L-fucose-1-phosphate and GTP. FPGT functions to reutilize the L-fucose that is produced uopn glycoprotein and glycolipid turnover.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which are essential interfaces for biological recognition processes. Fucosyltransferases (FucTs) catalyze the covalent association of fucose to different positional linkages on sugar acceptor molecules. The carbohydrate moieties that are generated are covalently attached to cell surfaces and are necessary to ensure a surface contour that satisfies a variety of physiological roles. FucT-XI is a 492 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 10 family. Localizing to Golgi apparatus, FucT-XI may act as a fucosyltransferase and exists as two alternatively spliced isoforms. The gene encoding FucT-XI maps to mouse chromosome 14 A3.

Supplier: Biotium

APTS is a very useful green fluorescent dye for labeling glycoproteins or sugar molecules in general. The labeling occurs via reductive amination which involves the formation of a Schiff base between the amine of APTS and the aldehyde or ketone of the sugar, followed by the reduction of the Schiff base linkage to a stable carbon-nitrogen bond. The multi-anionic nature of the dye makes it ideal for the studies of carbohydrate molecules by high resolution capillary electrophoresis.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesised by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesised by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.

Supplier: Bioss

This gene is a member of the beta-1,3-galactosyltransferase (beta3GalT) gene family. This family encodes type II membrane-bound glycoproteins with diverse enzymatic functions using different donor substrates (UDP-galactose and UDP-N-acetylglucosamine) and different acceptor sugars (N-acetylglucosamine, galactose, N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein coding sequence contained in a single exon. The beta3GalT proteins also contain conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during embryogenesis. By sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). The encoded protein of this gene does not use N-acetylglucosamine as an acceptor sugar at all. Multiple transcript variants that are alternatively spliced in the 5' UTR have been described; they all encode the same protein.