Skip to Content
MilliporeSigma
All Photos(2)

Documents

G1163

Sigma-Aldrich

O-Glycosidase from Streptococcus pneumoniae

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

Endo-α-N-acetylgalactosaminidase, O-Glycanase

Sign Into View Organizational & Contract Pricing
All Photos(2)

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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 Hong et al.
Journal of cancer research and clinical oncology, 127(9), 551-558 (2001-09-26)
To identify a new tumor-associated antigen, a monoclonal antibody, SC142, was produced by immunizing mice with a stomach cancer cell line. The tumor specificity of mAb SC142 was studied by immunohistochemical staining, and the biochemical characteristics of this new gastrointestinal
L Robertson et al.
Journal of reproduction and fertility, 120(2), 397-403 (2000-11-04)
This study demonstrates that carbohydrates play an essential role in sperm-egg interactions in birds. Sperm-egg interaction was measured in vitro as the ability of spermatozoa to hydrolyse a small hole in the inner perivitelline layer, the equivalent of the mammalian
Aimee E Stephenson et al.
Molecular microbiology, 43(1), 147-157 (2002-02-19)
Streptococcus parasanguis is a primary colonizer of the tooth surface and plays a pivotal role in the formation of dental plaque. The fimbriae of S. parasanguis are important in mediating adhesion to saliva-coated hydroxylapatite (SHA), an in vitro tooth adhesion
C Liu et al.
Journal of mass spectrometry : JMS, 32(1), 33-42 (1997-01-01)
A high-performance liquid chromatographic/electrospray mass spectrometric (HPLC/MS) technique is described for the characterization of the beta-subunit of the glycopeptide human chorionic gonadotropin (hCG). The beta-subunit of hCG was dissociated from the alpha-subunit using 0.1% trifluoroacetic acid (TFA) and separated by
View All Related Papers

Articles

O-Linked Glycan Strategies

While most N-linked oligosaccharides can be removed using PNGase F, a comparable enzyme for removing intact O-linked sugars has not been identified. Monosaccharides must be sequentially hydrolyzed by a series of exoglycosidases until only the Gal-β(1→3)-GalNAc core remains.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service