You Searched For: Udp-alpha-d-n-acetylgalactosamine,disodiumsalt


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Catalog Number: (80054-954)
Supplier: MilliporeSigma
Description: (UDP-GalNAc, sodium). White solid. Donor substrate for N-acetylgalactosaminyltransferases. A major terminal sugar of cyst wall of Giardia lamblia.

Supplier: Ambeed
Description: Udp-alpha-d-n-acetylgalactosamine,disodiumsalt, Purity: 98%, CAS Number: 108320-87-2, Appearance: Solid, Storage: Sealed in dry, Store in freezer, under -20C, Size: 25MG

Supplier: Ambeed
Description: Uridine-5′-diphosphogalactose disodium salt ≥98%

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Catalog Number: (10103-716)
Supplier: Prosci
Description: The GALNT13 protein is a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAcT; EC 2.4.1.41) family, which initiate O-linked glycosylation of mucins by the initial transfer of N-acetylgalactosamine (GalNAc) with an alpha-linkage to a serine or threonine residue.The GALNT13 protein is a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAcT; EC 2.4.1.41) family, which initiate O-linked glycosylation of mucins (see MUC3A, MIM 158371) by the initial transfer of N-acetylgalactosamine (GalNAc) with an alpha-linkage to a serine or threonine residue.


Catalog Number: (89359-076)
Supplier: Genetex
Description: GALNT12 is a member of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (EC 2.4.1.41), which catalyze the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to a hydroxyl amino acid on a polypeptide acceptor in the initial step of mucin-type O-linked protein glycosylation (Guo et al., 2002 [PubMed 12135769]).[supplied by OMIM]


Catalog Number: (10294-254)
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.


Catalog Number: (10294-250)
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.


Catalog Number: (10295-442)
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.


Catalog Number: (10293-952)
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.


Catalog Number: (10294-252)
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.


Catalog Number: (10295-546)
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.


Catalog Number: (10293-954)
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.


Catalog Number: (10293-956)
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.


Catalog Number: (10294-256)
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.


Catalog Number: (10294-258)
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.


Catalog Number: (10293-958)
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.


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