G1163
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:
UNSPSC Code:
12352204
EC Number:
232-888-2
NACRES:
NA.32
MDL number:
Recombinant:
expressed in E. coli
Concentration:
≥800 units/mL
recombinant
expressed in E. coli
conjugate
(O-linked)
form
buffered aqueous solution
mol wt
180 kDa
concentration
≥800 units/mL
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Related Categories
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.
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.
Other Notes
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.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
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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
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
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
A Shibuya
Pediatrics international : official journal of the Japan Pediatric Society, 43(6), 597-604 (2001-12-12)
Childhood hypoplastic anemia of unknown etiology had not existed until now. To assess pathophysiological differentiation in childhood hypoplastic anemia, we analyzed red cell membrane components in six children with hypoplastic anemia of unknown etiology. The six children all had chronic
Articles
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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Datasheet
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