57542 Results for: "Gal+beta(1-3)GalNAc-alpha-Thr"

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: TCI

GlcNAc-β-(1-3)[Neu5Ac-α-(2-6)]GalNAc-α-pNP ≥97.0% (by HPLC)

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: Bioss

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.

Supplier: TCI

GlcNAc-β-(1-3)GalNAc-ɑ-pNP ≥98.0% (by HPLC)

Supplier: ProSci Inc.

This gene encodes a member of the galactose-3-O-sulfotransferase protein family. The product of this gene catalyzes sulfonation by transferring a sulfate to the C-3' position of galactose residues in O-linked glycoproteins. This enzyme is highly specific for core 1 structures, with asialofetuin, Gal-beta-1,3-GalNAc and Gal-beta-1,3 (GlcNAc-beta-1,6)GalNAc being good substrates.

Supplier: TCI

Neu5Ac alpha(2-6)Gal beta(1-4)GlcNAc-beta-ethylamine ≥98.0% (by HPLC)

Supplier: TCI

Neu5Gc-α(2-3)Gal-β-MP glycoside ≥95.0% (by HPLC)

Supplier: TCI

Neu5Ac-α(2-3)Gal-β(1-4)Glc-β-pNP ≥97.0% (by HPLC)

Supplier: TCI

Neu5Gc-ɑ(2-6)Gal-β-MP glycoside ≥97.0% (by HPLC)

Supplier: TCI

Neu5Ac-ɑ(2-3)Gal-β-MP Glycoside ≥95.0% (by HPLC)

Supplier: TCI

Gal β(1-4)[Neu5Ac α(2-6)]GlcNAc-β-pNP ≥90.0% (by HPLC)

Supplier: TCI

Neu5Ac-α(2-6)Gal-β(1-3)GlcNAc-β-pNP ≥97.0% (by HPLC)

Supplier: TCI

Neu5Ac-ɑ(2-3)Gal-β(1-4)GlcNAc-β-pNP ≥95.0% (by HPLC)