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G1163

Sigma-Aldrich

O-Glycosidase from Streptococcus pneumoniae

recombinant, expressed in E. coli, buffered aqueous solution

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Synonym(s):
Endo-α-N-acetylgalactosaminidase, O-Glycanase
CAS Number:
9032-92-2
Enzyme Commission number:
3.2.1.97 (BRENDA, IUBMB)
EC Number:
232-888-2
MDL number:
MFCD00131003
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

200

conjugate

(O-linked)

form

buffered aqueous solution

mol wt

180 kDa

concentration

≥800 units/mL

shipped in

wet ice

storage temp.

2-8°C

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This Item
E9030A6805324716
O-Glycosidase from Streptococcus pneumoniae recombinant, expressed in E. coli, buffered aqueous solution

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G1163

O-Glycosidase from Streptococcus pneumoniae

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E9030

Endoglycoceramidase II from Rhodococcus sp.

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A6805

β-N-Acetylglucosaminidase from Streptococcus pneumoniae

Sigma-Aldrich

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324716

Endo-α-N-acetylgalactosaminidase, Streptococcus pneumoniae, Recombinant, E. coli

form

buffered aqueous solution

form

solution

form

buffered aqueous solution

form

liquid

mol wt

180 kDa

mol wt

58.9 kDa

mol wt

-

mol wt

-

concentration

≥800 units/mL

concentration

-

concentration

-

concentration

-

shipped in

wet ice

shipped in

dry ice

shipped in

wet ice

shipped in

wet ice

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

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 Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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
Ryoko Akai et al.
The Analyst, 128(5), 440-446 (2003-06-07)
O-Glycans (mucin type oligosaccharides) are ubiquitously found in various glycoproteins such as mucin-type glycoproteins on the surface of various digestive organs. In the present paper, we propose a method for detecting O-glycanase which catalyzes the hydrolysis of the O-glycan linkage
K Sonoda et al.
Cancer, 77(8), 1501-1509 (1996-04-15)
A large number of monoclonal antibodies (MoAbs) against human tumor cells have been generated and it has been shown that these MoAbs are useful tools in the diagnosis and treatment of cancer patients, as well as in the basic investigation
View All Related Papers

Articles

O-Linked Glycan Strategies

Learn about O-linked glycan strategies, such as the actions of O-glycosidase, how to remove di and trisialylation sialic acid residues, β-linked galactose, and N-acetylglucosamine, as well as other O-glycan modifications.

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