607 Results for: "Sugars, Amino Acids & Nucleotides"

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

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: MP Biomedicals

Adenosine 5′-monophosphate is a nucleotide that is used as a monomer in RNA. It is an ester of phosphoric acid and the nucleoside adenosine. AMP consists of a phosphate group, the sugar ribose, and the nucleobase adenine.

Supplier: Prosci

SLC35D3 Antibody: The solute carrier family SLC35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The novel protein SLC35D3 is highly homologous to SLC35D1 and SLC35D2, both of which transport UDP-glucuronic acid and UDP-N-acetylgalactosamine, suggesting that SLC35D3 is also involved in the transport of nucleotide sugars. It has been suggested that SLC35D3 regulates platelet dense granules, lysosome-related organelles which contain high concentrations of several biologically important low molecular weight molecules necessary for normal blood homeostasis.

Supplier: Prosci

SLC35D3 Antibody: The solute carrier family SLC35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The novel protein SLC35D3 is highly homologous to SLC35D1 and SLC35D2, both of which transport UDP-glucuronic acid and UDP-N-acetylgalactosamine, suggesting that SLC35D3 is also involved in the transport of nucleotide sugars. It has been suggested that SLC35D3 regulates platelet dense granules, lysosome-related organelles which contain high concentrations of several biologically important low molecular weight molecules necessary for normal blood homeostasis.

Supplier: Rockland Immunochemical

The solute carrier family SLC35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The novel protein SLC35D3 is highly homologous to SLC35D1 and SLC35D2, both of which transport UDP-glucuronic acid and UDP-N-acetylgalactosamine, suggesting that SLC35D3 is also involved in the transport of nucleotide sugars. It has been suggested that SLC35D3 regulates platelet dense granules, lysosome-related organelles which contain high concentrations of several biologically important low molecular weight molecules necessary for normal blood homeostasis.

Supplier: Prosci

SLC35D2 Antibody: The solute carrier family SLC35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident SLC family member SLC35D2 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. Its overexpression in transfected cells modulated cell surface heparin sulfate expression, suggesting that SLC35D2 is involved in heparin sulfate synthesis. SLC35D2-overexpressing cells also showed increased constitutive and hypotonic stress-stimulated release of UDP-GlcNAc, suggesting that SLC35D2 may be involved in UDP-sugar release and cell signaling.

Supplier: Prosci

Slc35D1 Antibody: The solute carrier family Slc35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident Slc family member Slc35D1 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. These molecules can serve as substrates for chondroitin sulfate biosynthesis and mice lacking the Slc35D1 gene developed a lethal form of skeletal dysplasia with severe shortening of limbs and facial structures. Examination of epiphyseal cartilage in these mice revealed a decreased proliferating zone with round chrondrocytes, scarce matrices, and reduced proteoglycan aggregates. Loss of function mutations in human Slc35D1 cause Schneckenbecken dysplasia, a severe skeletal dysplasia.

Supplier: Rockland Immunochemical

The solute carrier family SLC35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident SLC family member SLC35D2 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. Its overexpression in transfected cells modulated cell surface heparin sulfate expression, suggesting that SLC35D2 is involved in heparin sulfate synthesis. SLC35D2-overexpressing cells also showed increased constitutive and hypotonic stress-stimulated release of UDP-GlcNAc, suggesting that SLC35D2 may be involved in UDP-sugar release and cell signaling.

Supplier: Prosci

SLC35D2 Antibody: The solute carrier family SLC35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident SLC family member SLC35D2 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. Its overexpression in transfected cells modulated cell surface heparin sulfate expression, suggesting that SLC35D2 is involved in heparin sulfate synthesis. SLC35D2-overexpressing cells also showed increased constitutive and hypotonic stress-stimulated release of UDP-GlcNAc, suggesting that SLC35D2 may be involved in UDP-sugar release and cell signaling.

Supplier: Prosci

Slc35D1 Antibody: The solute carrier family Slc35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident Slc family member Slc35D1 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. These molecules can serve as substrates for chondroitin sulfate biosynthesis and mice lacking the Slc35D1 gene developed a lethal form of skeletal dysplasia with severe shortening of limbs and facial structures. Examination of epiphyseal cartilage in these mice revealed a decreased proliferating zone with round chrondrocytes, scarce matrices, and reduced proteoglycan aggregates. Loss of function mutations in human Slc35D1 cause Schneckenbecken dysplasia, a severe skeletal dysplasia.

Supplier: Prosci

Slc35D1 Antibody: The solute carrier family Slc35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident Slc family member Slc35D1 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. These molecules can serve as substrates for chondroitin sulfate biosynthesis and mice lacking the Slc35D1 gene developed a lethal form of skeletal dysplasia with severe shortening of limbs and facial structures. Examination of epiphyseal cartilage in these mice revealed a decreased proliferating zone with round chrondrocytes, scarce matrices, and reduced proteoglycan aggregates. Loss of function mutations in human Slc35D1 cause Schneckenbecken dysplasia, a severe skeletal dysplasia.

Supplier: Rockland Immunochemical

The solute carrier family Slc35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident Slc family member Slc35D1 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. These molecules can serve as substrates for chondroitin sulfate biosynthesis and mice lacking the Slc35D1 gene developed a lethal form of skeletal dysplasia with severe shortening of limbs and facial structures. Examination of epiphyseal cartilage in these mice revealed a decreased proliferating zone with round chrondrocytes, scarce matrices, and reduced proteoglycan aggregates. Loss of function mutations in human Slc35D1 cause Schneckenbecken dysplasia, a severe skeletal dysplasia.

Supplier: Rockland Immunochemical

The solute carrier family Slc35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident Slc family member Slc35D1 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. These molecules can serve as substrates for chondroitin sulfate biosynthesis and mice lacking the Slc35D1 gene developed a lethal form of skeletal dysplasia with severe shortening of limbs and facial structures. Examination of epiphyseal cartilage in these mice revealed a decreased proliferating zone with round chrondrocytes, scarce matrices, and reduced proteoglycan aggregates. Loss of function mutations in human Slc35D1 cause Schneckenbecken dysplasia, a severe skeletal dysplasia.

Supplier: Prosci

Slc35D1 Antibody: The solute carrier family Slc35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident Slc family member Slc35D1 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. These molecules can serve as substrates for chondroitin sulfate biosynthesis and mice lacking the Slc35D1 gene developed a lethal form of skeletal dysplasia with severe shortening of limbs and facial structures. Examination of epiphyseal cartilage in these mice revealed a decreased proliferating zone with round chrondrocytes, scarce matrices, and reduced proteoglycan aggregates. Loss of function mutations in human Slc35D1 cause Schneckenbecken dysplasia, a severe skeletal dysplasia.

Supplier: Prosci

Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity.

Supplier: Thermo Scientific Chemicals

Dextrin, precipitated

Supplier: Thermo Scientific Chemicals

Cytidine 99%

Supplier: Thermo Scientific Chemicals

98% 5G

Supplier: Thermo Scientific Chemicals

5-Carbethoxyuracil 98%

Supplier: Thermo Scientific Chemicals

L-Isoserine 98%

Supplier: Thermo Scientific Chemicals

Oleanolic acid 97%, solid

Supplier: Thermo Scientific Chemicals

2'-Deoxyinosine 98+%

Supplier: Thermo Scientific Chemicals

Cellulose, microcrystalline

Supplier: Thermo Scientific Chemicals

L(+)-Lyxose 99%

Supplier: Thermo Scientific Chemicals

α-D-Talose 97%