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G0413

Sigma-Aldrich

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

recombinant, expressed in E. coli, buffered aqueous solution

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About This Item

Número de CAS:
9031-11-2
Comisión internacional de enzimas:
3.2.1.23 (BRENDA, IUBMB)
Número MDL:
MFCD01092684
Código UNSPSC:
12352204
NACRES:
NA.32

recombinante

expressed in E. coli

Nivel de calidad

100

Formulario

buffered aqueous solution

actividad específica

≥6 units/mg protein

envase

vial of 0.06 unit

Nº de acceso UniProt

P16278

Condiciones de envío

wet ice

temp. de almacenamiento

2-8°C

Información sobre el gen

human ... GLB1(2720)

Categorías relacionadas

Descripción general

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.

Aplicación

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).

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

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

Forma física

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

Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
MKCW3644
MKCW2119
MKCW6649
MKCT4022
MKCT1016

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S K Bhaumik et al.
Glycoconjugate journal, 25(5), 459-472 (2008-01-17)
Protozoan parasites of the genus Leishmania are the causative agent of leishmaniasis, a disease whose manifestations in humans range from mild cutaneous lesions to fatal visceral infections. Human visceral leishmaniasis is caused by Leishmania donovani. Long-term culture in vitro leads
TLR4 and NKT cell synergy in immunotherapy against visceral leishmaniasis
Karmakar S, et al.
PLoS Pathogens, 8(4), 79-79 (2012)
Qayyum Husain
Critical reviews in biotechnology, 30(1), 41-62 (2010-02-11)
Beta galactosidases have been obtained from microorganisms such as fungi, bacteria and yeasts; plants, animals cells, and from recombinant sources. The enzyme has two main applications; the removal of lactose from milk products for lactose intolerant people and the production
beta Galactosidases and their potential applications: a review
Husain Q
Critical Reviews in Biotechnology, 30(1), 41-62 (2010)
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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