Skip to Content
MilliporeSigma

Skip To

G0413

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

recombinant, expressed in E. coli, buffered aqueous solution

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View
Size/SKUAvailabilityPrice
1 vial

Available to ship TODAYfromMILWAUKEE

$676.00
$700.00

About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
MDL number:
Specific activity:
≥6 units/mg protein
Recombinant:
expressed in E. coli

$700.00

Web-Only Promotion

Available to ship TODAYDetails


​
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist


recombinant

expressed in E. coli

Quality Segment

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.

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.

Compare Similar Items

View Full Comparison

Show Differences

1 of 1

This Item
G0288AB1211G1288
description

recombinant, expressed in E. coli, buffered aqueous solution

description

recombinant, expressed in E. coli, buffered aqueous solution

description

Chemicon®, from rabbit

description

recombinant, expressed in E. coli, buffered aqueous solution

specific activity

≥6 units/mg protein

specific activity

≥120 units/mg protein

specific activity

-

specific activity

≥70 units/mg protein

Gene Information

human ... GLB1(2720)

Gene Information

human ... GLB1(2720)

Gene Information

human ... GLB1(2720)

Gene Information

-

form

buffered aqueous solution

form

buffered aqueous solution

form

-

form

buffered aqueous solution

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

recombinant

expressed in E. coli

UniProt accession no.

P16278

UniProt accession no.

P16278

UniProt accession no.

P16278

UniProt accession no.

-

shipped in

wet ice

shipped in

wet ice

shipped in

-

shipped in

wet ice


Storage Class

10 - Combustible liquids

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

Pictograms

Health hazard

Signal Word

Danger

Hazard Codes

Precautionary Statements

Hazard Classifications

Resp. Sens. 1



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

It looks like we've run into a problem, but you can still download Certificates of Analysis from our Documents section.

If you need assistance, please contact Customer Support

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library




Questions

Reviews

No rating value

Active Filters