Supplier: Bioss

Glycosyltransferases that mediate the region and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyse the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins. Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking. Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

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 is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis b is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6). Blood Group Lewis a is a carbohydrate determinant carried on both glycolipids and glycoproteins.

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

Supplier: Bioss

Glycosyltransferases that mediate the regio- and stereoselective transfer of sugars, such as the fucosyltransferases, determine cell surface-carbohydrate profiles, which is an essential interface for biological recognition processes. Fucosyltransferases catalyze the covalent association of fucose to different positional linkages in sugar acceptor molecules. The carbohydrate moieties generated and covalently attached to cell surfaces are necessary to ensure a surface contour that satisfies physiological roles, which are reliant on adhesion molecules such as Selectins (1-3). Hematopoietic lineages rely on Fucosyltransferases to confer a surface carbohydrate phenotype, which mediates proper cell adhesion molecule recruitment and cell trafficking (4-6).

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

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.