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

Name: β(1→4)-Galactosidase, positionally specific from <I>Streptococcus pneumoniae</I>
Brand: SIGMA
Price: 676 USD
Availability: InStock

recombinant, expressed in E. coli, buffered aqueous solution

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Pack Size	SKU	Availability	Price
1 vial		Available to ship TODAYfromMILWAUKEE	$676.00

About This Item

CAS Number:

9031-11-2

UNSPSC Code:

12352204

NACRES:

NA.32

EC Number:

3.2.1.23 (BRENDA, IUBMB)

MDL number:

MFCD01092684

Specific activity:

≥6 units/mg protein

Recombinant:

expressed in E. coli

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recombinant

expressed in E. coli

Quality Level

100

form

buffered aqueous solution

specific activity

≥6 units/mg protein

packaging

vial of 0.06 unit

UniProt accession no.

P16278

shipped in

wet ice

storage temp.

2-8°C

Gene Information

human ... GLB1(2720)

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Proteins & Enzymes

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Show Differences

1 of 1

This Item	G1288	G6008	G5635
Sigma-Aldrich G0413 β(1→4)-Galactosidase, positionally specific from Streptococcus pneumoniae	Sigma-Aldrich G1288 β-(1→3,4,6)-Galactosidase, positionally specific	Sigma-Aldrich G6008 β-Galactosidase from Escherichia coli	Sigma-Aldrich G5635 β-Galactosidase from Escherichia coli
specific activity ≥6 units/mg protein	specific activity ≥70 units/mg protein	specific activity ≥250 units/mg protein	specific activity ≥500 units/mg protein
Gene Information human ... GLB1(2720)	Gene Information -	Gene Information -	Gene Information -
form buffered aqueous solution	form buffered aqueous solution	form lyophilized powder	form lyophilized powder
recombinant expressed in E. coli	recombinant expressed in E. coli	recombinant -	recombinant -
shipped in wet ice	shipped in wet ice	shipped in wet ice	shipped in -
storage temp. 2-8°C	storage temp. 2-8°C	storage temp. −20°C	storage temp. −20°C

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.

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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

pictograms

GHS08

signalword

Danger

hcodes

H334

pcodes

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

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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)

Sources of beta-galactosidase and its applications in food industry

Saqib S, et al.

3 Biotech, 7(1), 79-79 (2017)

Sources of β-galactosidase and its applications in food industry.

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

TLR4 and NKT cell synergy in immunotherapy against visceral leishmaniasis

Karmakar S, et al.

PLoS Pathogens, 8(4), 79-79 (2012)

Isomer and glycomer complexities of core GlcNAcs in Caenorhabditis elegans.

Andrew J Hanneman et al.

Glycobiology, 16(9), 874-890 (2006-06-14)

Analysis of protein glycosylation within the nematode Caenorhabditis elegans has revealed an abundant and unreported set of core chitobiose modifications (CCMs) to N-linked glycans. With hydrazine release, an array of glycomers and isobars were detected with hexose extensions on the

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Global Trade Item Number

SKU	GTIN
G0413-1VL-PW	04061832852713
G0413-1VL	04061838078971

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