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G1163

Sigma-Aldrich

O-Glycosidase from Streptococcus pneumoniae

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

Endo-α-N-acetylgalactosaminidase, O-Glycanase

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About This Item

CAS Number:
9032-92-2
Enzyme Commission number:
3.2.1.97 (BRENDA, IUBMB)
EC Number:
232-888-2
MDL number:
MFCD00131003
UNSPSC Code:
12352204
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

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
G H Carpenter et al.
Oral microbiology and immunology, 14(5), 309-315 (1999-11-07)
Interactions between salivary glycoproteins and many oral bacteria have been shown to depend on O-linked glycans on salivary glycoproteins. Basic proline-rich proteins form the largest group of proteins within human parotid saliva. In the present study human parotid salivary glycoproteins
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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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.

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.

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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