G1163
O-Glycosidase from Streptococcus pneumoniae
recombinant, expressed in E. coli, buffered aqueous solution
Synonym(s):
Endo-α-N-acetylgalactosaminidase, O-Glycanase
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
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 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
Regulatory Information
常规特殊物品
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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
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
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:
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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