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Merck

G0413

Sigma-Aldrich

β(1→4)-Galactosidase, positionally specific from Streptococcus pneumoniae

recombinant, expressed in E. coli, buffered aqueous solution

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CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

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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)

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G0288G6008G3153
Gene Information

human ... GLB1(2720)

Gene Information

human ... GLB1(2720)

Gene Information

-

Gene Information

-

specific activity

≥6 units/mg protein

specific activity

≥120 units/mg protein

specific activity

≥250 units/mg protein

specific activity

≥500 units/mg protein

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

recombinant

expressed in E. coli

form

buffered aqueous solution

form

buffered aqueous solution

form

lyophilized powder

form

lyophilized powder

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

-

UniProt accession no.

P16278

UniProt accession no.

P16278

UniProt accession no.

-

UniProt accession no.

-

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.[1] 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.[2]

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.[3]
  • for the digestion of radioactive oligosaccharides.[4]
  • as a position-specific enzymeto study its effects on the virulence profile of avirulent Leishmania donovani clone (A-LD).[5]

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.[1]

Physical form

Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl

Other Notes

One unit will hydrolyze 1 μmole of p-nitrophenyl β-D-galactopyranoside per min at pH 5.0 at 37 °C.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Virulence attenuation of a UDP-galactose/N-acetylglucosamine beta1, 4 galactosyltransferase expressing Leishmania donovani promastigote
Bhaumik, SK , et al.
Glycoconjugate Journal, 25(5), 459-472 (2008)
Shaima Saqib et al.
3 Biotech, 7(1), 79-79 (2017-05-14)
The enzyme β-galactosidases have been isolated from various sources such as bacteria, fungi, yeast, vegetables, and recombinant sources. This enzyme holds importance due to its wide applications in food industries to manufacture lactose-hydrolyzed products for lactose-intolerant people and the formation
Sources of beta-galactosidase and its applications in food industry
Saqib S, et al.
3 Biotech, 7(1), 79-79 (2017)
Isomer and glycomer complexities of core GlcNAcs in Caenorhabditis elegans
Hanneman A J, et al.
Glycobiology, 16(9), 874-890 (2006)
TLR4 and NKT cell synergy in immunotherapy against visceral leishmaniasis
Karmakar S, et al.
PLoS Pathogens, 8(4), 79-79 (2012)

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