You Searched For: D-Galactosamine+pentaacetate

Catalog Number: (BOSSBS-13452R-A647)

Supplier: Bioss

Description: The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13452R-CY7)

Supplier: Bioss

Description: The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-6989R)

Supplier: Bioss

Description: H6PD (hexose-6-phosphate dehydrogenase, GDH/6PGL endoplasmic bifunctional protein) is a 789 amino acid protein encoded by the human gene H6PD. The N-terminal section of H6PD belongs to the glucose-6-phosphate dehydrogenase family, while the C-terminal section belongs to the glucosamine/galactosamine-6-phosphate isomerase family, 6-phosphogluconolactonase subfamily. H6PD is responsible primarily for the oxidation of glucose-6-phosphate and glucose. It also oxidizes other hexose-6-phosphates. H6PD catalyzes the conversion of glucose 6-phosphate to 6-phosphogluconolactone within the lumen of the endoplasmic reticulum, thereby generating reduced nicotinamide adenine dinucleotide phosphate. Reduced nicotinamide adenine dinucleotide phosphate is a necessary cofactor for the reductase activity of 11∫-hydroxysteroid dehydrogenase type 1, which converts hormonally inactive cortisone to active cortisol (in rodents, 11-dehydrocorticosterone to corticosterone).

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13270R-A555)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosaminyl) to serine and threonine residues of various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T10 (Polypeptide N-acetylgalactosaminyltransferase 10), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, is a 603 amino acid single-pass type II membrane protein that prefers Muc5Ac and EA2 peptide substrates. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T10 is widely expressed, with highest levels found in small intestine. There are four isoforms of GalNAc-T10 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13271R-A488)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T11 (Polypeptide N-acetylgalactosaminyltransferase 11), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, is a 608 amino acid protein that catalyzes glycosylation of Muc1, Muc4.1 and EA2, though it does not display enzymatic preference for erythropoitein. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T11 is highly expressed in kidney tubules, though it is not expressed in glomeruli. There are two isoforms of GalNAc-T11 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13270R-A680)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosaminyl) to serine and threonine residues of various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T10 (Polypeptide N-acetylgalactosaminyltransferase 10), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, is a 603 amino acid single-pass type II membrane protein that prefers Muc5Ac and EA2 peptide substrates. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T10 is widely expressed, with highest levels found in small intestine. There are four isoforms of GalNAc-T10 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13271R-A555)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T11 (Polypeptide N-acetylgalactosaminyltransferase 11), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, is a 608 amino acid protein that catalyzes glycosylation of Muc1, Muc4.1 and EA2, though it does not display enzymatic preference for erythropoitein. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T11 is highly expressed in kidney tubules, though it is not expressed in glomeruli. There are two isoforms of GalNAc-T11 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (MOLE69522692-1KG)

Supplier: Molekula

Description: Diethylenetriaminepentaacetic acid

UOM: 1 * 1 kg

 This is a MarketSource item. Additional charges may apply

Catalog Number: (BOSSBS-13274R-A488)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13274R-A350)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13270R-CY3)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosaminyl) to serine and threonine residues of various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T10 (Polypeptide N-acetylgalactosaminyltransferase 10), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, is a 603 amino acid single-pass type II membrane protein that prefers Muc5Ac and EA2 peptide substrates. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T10 is widely expressed, with highest levels found in small intestine. There are four isoforms of GalNAc-T10 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13271R-CY7)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T11 (Polypeptide N-acetylgalactosaminyltransferase 11), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, is a 608 amino acid protein that catalyzes glycosylation of Muc1, Muc4.1 and EA2, though it does not display enzymatic preference for erythropoitein. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T11 is highly expressed in kidney tubules, though it is not expressed in glomeruli. There are two isoforms of GalNAc-T11 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13270R-FITC)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosaminyl) to serine and threonine residues of various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T10 (Polypeptide N-acetylgalactosaminyltransferase 10), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, is a 603 amino acid single-pass type II membrane protein that prefers Muc5Ac and EA2 peptide substrates. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T10 is widely expressed, with highest levels found in small intestine. There are four isoforms of GalNAc-T10 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13271R-HRP)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T11 (Polypeptide N-acetylgalactosaminyltransferase 11), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, is a 608 amino acid protein that catalyzes glycosylation of Muc1, Muc4.1 and EA2, though it does not display enzymatic preference for erythropoitein. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T11 is highly expressed in kidney tubules, though it is not expressed in glomeruli. There are two isoforms of GalNAc-T11 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13274R-CY5)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T13 (Polypeptide N-acetylgalactosaminyltransferase 13), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, is a 556 amino acid protein that displays much stronger enzymatic activity than GalNAc-1 towards GalNAc transfer to mucin peptides such as Muc5a and Muc7. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. With specific expression in the central nervous system, GalNAc-T13 may be responsible for the synthesis of Tn antigen in neuronal cells, which is a universal carcinoma marker on malignant cells.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13270R-A488)

Supplier: Bioss

Description: The UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes are substrate-specific proteins that catalyze the transfer of GalNAc (N-acetylgalactosaminyl) to serine and threonine residues of various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T10 (Polypeptide N-acetylgalactosaminyltransferase 10), also known as UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10, is a 603 amino acid single-pass type II membrane protein that prefers Muc5Ac and EA2 peptide substrates. The N-terminal domain is involved in substrate binding and manganese coordination, while the C-terminal domain is involved in UDP-Gal binding and catalytic reaction. GalNAc-T10 is widely expressed, with highest levels found in small intestine. There are four isoforms of GalNAc-T10 that are produced as a result of alternative splicing events.

UOM: 1 * 100 µl