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Merck

G1163

Sigma-Aldrich

O-Glycosidase from Streptococcus pneumoniae

recombinant, expressed in E. coli, buffered aqueous solution

Sinónimos:

Endo-α-N-acetylgalactosaminidase, O-Glycanase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

conjugate

(O-linked)

form

buffered aqueous solution

mol wt

180 kDa

concentration

≥800 units/mL

shipped in

wet ice

storage temp.

2-8°C

Biochem/physiol Actions

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..

Packaging

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

Unit Definition

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.

Physical form

Solution in 50 mM sodium phosphate, pH 7.5

Analysis Note

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

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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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
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 Yamini Shrivastava et al.
Journal of biomolecular structure & dynamics, 21(5), 671-680 (2004-02-11)
In the present study, the impact of chromium(III) complexes ([Cr(salen)(H2O)2](+) (1), [Cr(en)3]3+ (2) and [Cr(EDTA)(H2O)]- (3)) on the biophysical properties of mucin like specific viscosity, zeta potential and particle size has been investigated. It is evident from the present investigation
Tongzhong Ju et al.
Glycobiology, 16(10), 947-958 (2006-06-10)
The common O-glycan core structure in animal glycoproteins is the core 1 disaccharide Galbeta1-3GalNAcalpha1-Ser/Thr, which is generated by the addition of Gal to GalNAcalpha1-Ser/Thr by core 1 UDP-alpha-galactose (UDP-Gal):GalNAcalpha1-Ser/Thr beta1,3-galactosyltransferase (core 1 beta3-Gal-T or T-synthase, EC2.4.1.122). Although O-glycans play important

Artículos

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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