You Searched For: Manganese+(III)+acetate+dihydrate

Catalog Number: (BOSSBS-13273R-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-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

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-13274R-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-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-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-13273R-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-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

UOM: 1 * 100 µl

Supplier: FRITSCH

Description: Moving crushing jaw, manganese steel, Manganese steel, For: PULVERISETTE 1, Model II

Catalog Number: (BOSSBS-13273R-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-acetylgalactosamine) to serine and threonine residues onto various proteins, thereby initiating mucin-type O-linked glycosylation in the Golgi apparatus. GalNAc-T1, also known as GALNT1 (Polypeptide N-acetylgalactosaminyltransferase 1), is a ubiquitously expressed 559 amino acid single-pass type II membrane protein that localizes to the Golgi apparatus and, like other GalNAc-Ts, contains a stem region and a C-terminal ricin/lectin-like domain. GalNAc-T1 catalyzes the first reaction in O-linked oligosaccharide biosynthesis, namely the transfer of an N-acetyl-D-galactosamine residue to a protein acceptor. GalNAc-T1 uses calcium and manganese as cofactors. Due to alternative splicing events, two GalNAc-T1 isoforms are expressed.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13271R-A750)

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-A647)

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

Supplier: APOLLO SCIENTIFIC

Description: 3H-Heptafluoro-2,2,4,4-tetrahydroxypentane 97%

Supplier: Hach

Description: Standard solutions for accuracy checks in manganese determinations.

Catalog Number: (HACH2243300)

Supplier: Hach

Description: Reagent set used for determination of manganese by the PAN method.

UOM: 1 * 100 Tests

Catalog Number: (BOSSBS-13271R-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-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