G0413
β(1→4)-Galactosidase, positionally specific from Streptococcus pneumoniae
recombinant, expressed in E. coli, buffered aqueous solution
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32
Recommended Products
recombinant
expressed in E. coli
Quality Level
form
buffered aqueous solution
specific activity
≥6 units/mg protein
packaging
vial of 0.06 unit
UniProt accession no.
shipped in
wet ice
storage temp.
2-8°C
Gene Information
human ... GLB1(2720)
General description
β-Galactosidase is present in bacteria, fungi, yeast and animal organs. It is also found in fruits, such as apples, almonds and apricots. β-Galactosidase is a tetramer and is made up of four polypeptide chains consisting of amino acids that assemble to form five structural domains. The domains are jelly roll barrel, a central domain that serves as an active site and the remaining domains are composed of β-sandwich and fibronectin.
Application
β(1→4)-Galactosidase, positionally specific from Streptococcus pneumonia has been used:
- as a position-specific enzyme to study its effects in the terminal galactosylation with protective efficacy of glycosphingolipid (GSPL) in mice.
- for the digestion of radioactive oligosaccharides.
- as a position-specific enzymeto study its effects on the virulence profile of avirulent Leishmania donovani clone (A-LD).
Biochem/physiol Actions
β-Galactosidase plays a role in hydrolyzing the D-galactosyl moieties in oligosaccharides, polymers and secondary metabolites. It is widely applicable in the dairy industry to remove lactose from milk and dairy products for the benefit of lactose-intolerant individuals. β-Galactosidase is also applicable in the food industry to improve the sweetness, flavor and solubility.
Unit Definition
One unit will hydrolyze 1 μmole of p-nitrophenyl β-D-galactopyranoside per min at pH 5.0 at 37 °C.
Physical form
Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl
Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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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