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Principaux documents

G1163

Sigma-Aldrich

O-Glycosidase from Streptococcus pneumoniae

recombinant, expressed in E. coli, buffered aqueous solution

Synonyme(s) :

Endo-α-N-acetylgalactosaminidase, O-Glycanase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32
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Produit recombinant

expressed in E. coli

Niveau de qualité

Conjugué

(O-linked)

Forme

buffered aqueous solution

Poids mol.

180 kDa

Concentration

≥800 units/mL

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Actions biochimiques/physiologiques

Releases unsubstituted Ser- and Thr-linked β-Gal-(1→3)-α-GalNAc (Core 1 type O-glycan) from glycoproteins. Substitutions of the disaccharide core with sialic acid, lactosamine (galactose-N-acetyl glucosamine), or fucose will block hydrolysis and prevent the liberation of the oligosaccharide from the protein. Pretreament with glycolytic enzymes to remove substituent saccharides from the O-glycan may be needed prior to cleavage using O-glycosidase..

Conditionnement

Supplied with 5× Reaction Buffer, 250 mM NaH2PO4 pH 5.0.

Définition de l'unité

One unit will hydrolyze 1 μmole of p-nitrophenyl galacto-N-bioside (β-Gal-(1→3)-α-GalNAc-1→ΟC6H4NO2) per min at 37 °C at pH 6.5.

Forme physique

Solution in 50 mM sodium phosphate, pH 7.5

Remarque sur l'analyse

Screened for presence of: β-galactosidase, α-mannosidase, β-hexosaminidase, α-fucosidase, neuraminidase, and proteases. See Certificate of Analysis for lot specific information.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

I Brockhausen
Biochimica et biophysica acta, 1473(1), 67-95 (1999-12-02)
Glycoproteins with O-glycosidically linked carbohydrate chains of complex structures and functions are found in secretions and on the cell surfaces of cancer cells. The structures of O-glycans are often unusual or abnormal in cancer, and greatly contribute to the phenotype
Nelia A Tobey et al.
Digestive diseases and sciences, 55(7), 1856-1865 (2010-05-27)
The structures that contribute to shunt resistance (Rs) in esophageal epithelium are incompletely understood, with 35-40% of Rs known to be calcium-dependent, reflecting the role of e-cadherin. Two calcium-independent candidates for the remaining approximately 60% of Rs have been identified:
Roudabeh J Jamasbi et al.
Hybridoma and hybridomics, 22(6), 367-376 (2003-12-20)
A mouse monoclonal antibody (MAb-9) produced by immunization with a human esophageal carcinoma cell line, TE-2 (derived from undifferentiated squamous cell carcinoma) reacted specifically with about 30% of esophageal carcinoma cell lines and tissue sections from clinical samples. MAb-9 showed
A Shibuya
Pediatrics international : official journal of the Japan Pediatric Society, 43(6), 597-604 (2001-12-12)
Childhood hypoplastic anemia of unknown etiology had not existed until now. To assess pathophysiological differentiation in childhood hypoplastic anemia, we analyzed red cell membrane components in six children with hypoplastic anemia of unknown etiology. The six children all had chronic
K M Davis et al.
Protein expression and purification, 8(1), 57-67 (1996-08-01)
Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22-kDa, O-glycosylated protein. Because recombinant expression systems permitting a detailed analysis of the functional significance of HB-EGF glycosylation have not been described, a recombinant vaccinia virus designed to express HB-EGF was

Articles

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

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