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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:
9032-92-2
Numéro de classification (Commission des enzymes):
3.2.1.97 (BRENDA, IUBMB)
Numéro CE :
232-888-2
Numéro MDL:
MFCD00131003
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in E. coli

Niveau de qualité

200

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

Catégories apparentées

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)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
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:
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
H Miyata et al.
Okajimas folia anatomica Japonica, 78(4), 129-140 (2002-01-05)
The distribution or localization of glycoconjugates in rat cerebellar cortex was investigated with 26 different kinds of lectins observed by light and electron microscopy. In paraffin-embedded tissues, PHA-L, PHA-E, DSA, WGA, ConA, LEA, LCA, PSA, and RCA-I, which mainly recognize
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
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Articles

O-Linked Glycan Strategies

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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