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Catalog Number: (10295-544)
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.


Catalog Number: (10293-950)
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: (10295-440)
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.


Catalog Number: (10103-054)
Supplier: Prosci
Description: GALNT4 catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. In vitro, the encoded protein can complement other GalNAc-Ts in the complete O-glycosylation of the mucin-1 tandem repeat and can O-glycosylate the P-selectin glycoprotein ligand-1 molecule. The coding region of this gene is contained within a single exon.


Catalog Number: (76010-818)
Supplier: Prosci
Description: Glycosylation of proteins affects cell-cell interaction, interactions with the matrix, and the functions of intracellular molecules. ST6GALNAC1 transfers a sialic acid, N-acetylneuraminic acid (NeuAc), in an alpha-2,6 linkage to O-linked GalNAc residues. The cancer-associated sialyl-Tn (sTn) antigen is formed by ST6GALNAC1-catalyzed sialylation of GalNAc residues on mucins (Ikehara et al., 1999 [PubMed 10536037]; Sewell et al., 2006 [PubMed 16319059]).


Catalog Number: (10110-250)
Supplier: Prosci
Description: ST6GALNAC4 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. ST6GALNAC4 prefers glycoproteins rather than glycolipids as substrates and shows restricted substrate specificity, utilizing only the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc. In addition, it is involved in the synthesis of ganglioside GD1A from GM1B. ST6GALNAC4 is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. It is a member of glycosyltransferase family 29.The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein prefers glycoproteins rather than glycolipids as substrates and shows restricted substrate specificity, utilizing only the trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,3-GalNAc. In addition, it is involved in the synthesis of ganglioside GD1A from GM1B. The encoded protein is normally found in the Golgi apparatus but can be proteolytically processed to a soluble form. This protein is a member of glycosyltransferase family 29. Transcript variants encoding different isoforms have been found for this gene.


Catalog Number: (10295-398)
Supplier: Bioss
Description: GBGT1 is a 347 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 6 family. Localizing to the golgi apparatus membrane, GBGT1 is widely expressed, with high levels found in placenta, ovary and peripheral blood leukocyte, and lower levels expressed in liver, thymus and testis. GBGT1 utilizes manganese as a cofactor, and assists in the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to various substrates, resulting in the formation of glycolipids. Glycolipids are present in most eukaryotic cells and may assist in the adherence of certain pathogens. Existing as two alternatively spliced isoforms, the gene encoding GBGT1 maps to human chromosome 9q34.2 and mouse chromosome 2 A3.


Catalog Number: (10295-402)
Supplier: Bioss
Description: GBGT1 is a 347 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 6 family. Localizing to the golgi apparatus membrane, GBGT1 is widely expressed, with high levels found in placenta, ovary and peripheral blood leukocyte, and lower levels expressed in liver, thymus and testis. GBGT1 utilizes manganese as a cofactor, and assists in the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to various substrates, resulting in the formation of glycolipids. Glycolipids are present in most eukaryotic cells and may assist in the adherence of certain pathogens. Existing as two alternatively spliced isoforms, the gene encoding GBGT1 maps to human chromosome 9q34.2 and mouse chromosome 2 A3.


Catalog Number: (10295-400)
Supplier: Bioss
Description: GBGT1 is a 347 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 6 family. Localizing to the golgi apparatus membrane, GBGT1 is widely expressed, with high levels found in placenta, ovary and peripheral blood leukocyte, and lower levels expressed in liver, thymus and testis. GBGT1 utilizes manganese as a cofactor, and assists in the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to various substrates, resulting in the formation of glycolipids. Glycolipids are present in most eukaryotic cells and may assist in the adherence of certain pathogens. Existing as two alternatively spliced isoforms, the gene encoding GBGT1 maps to human chromosome 9q34.2 and mouse chromosome 2 A3.


Catalog Number: (10295-396)
Supplier: Bioss
Description: GBGT1 is a 347 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 6 family. Localizing to the golgi apparatus membrane, GBGT1 is widely expressed, with high levels found in placenta, ovary and peripheral blood leukocyte, and lower levels expressed in liver, thymus and testis. GBGT1 utilizes manganese as a cofactor, and assists in the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to various substrates, resulting in the formation of glycolipids. Glycolipids are present in most eukaryotic cells and may assist in the adherence of certain pathogens. Existing as two alternatively spliced isoforms, the gene encoding GBGT1 maps to human chromosome 9q34.2 and mouse chromosome 2 A3.


Catalog Number: (80502-554)
Supplier: MilliporeSigma
Description: Gangliosides are highly purified sialic acid-containing glycolipids that are useful as markers of various cell types and antigens. Prepared from tissue of individuals that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Catalog Number: (10295-394)
Supplier: Bioss
Description: GBGT1 is a 347 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 6 family. Localizing to the golgi apparatus membrane, GBGT1 is widely expressed, with high levels found in placenta, ovary and peripheral blood leukocyte, and lower levels expressed in liver, thymus and testis. GBGT1 utilizes manganese as a cofactor, and assists in the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to various substrates, resulting in the formation of glycolipids. Glycolipids are present in most eukaryotic cells and may assist in the adherence of certain pathogens. Existing as two alternatively spliced isoforms, the gene encoding GBGT1 maps to human chromosome 9q34.2 and mouse chromosome 2 A3.


Catalog Number: (10295-754)
Supplier: Bioss
Description: GBGT1 is a 347 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 6 family. Localizing to the golgi apparatus membrane, GBGT1 is widely expressed, with high levels found in placenta, ovary and peripheral blood leukocyte, and lower levels expressed in liver, thymus and testis. GBGT1 utilizes manganese as a cofactor, and assists in the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to various substrates, resulting in the formation of glycolipids. Glycolipids are present in most eukaryotic cells and may assist in the adherence of certain pathogens. Existing as two alternatively spliced isoforms, the gene encoding GBGT1 maps to human chromosome 9q34.2 and mouse chromosome 2 A3.


Catalog Number: (76084-478)
Supplier: Bioss
Description: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation. It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling. Has some overlapping function with SIAH2. Induces apoptosis in cooperation with PEG3. Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins.


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