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G7163

Sigma-Aldrich

α-Galactosidase, positionally specific from Escherichia coli

recombinant, expressed in E. coli, buffered aqueous solution

Synonyme(s) :

1,6-alpha-D-galactoside galactohydrolase, alpha-Galactosidase, melibiase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in E. coli

Niveau de qualité

Forme

buffered aqueous solution

Activité spécifique

≥20 units/mg protein

Poids mol.

80 kDa

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Informations sur le gène

Escherichia coli CFT073 ... melA(1037886)

Actions biochimiques/physiologiques

Cleaves α(1→3)- and α(1→6)-linked, non-reducing terminal galactose from complex carbohydrates and glycoproteins. It is particularly efficient for removing α-linked galactose under conditions where the pH must be neutral or above, for example, with live cells.

Définition de l'unité

One unit will hydrolyze 1 μmole of p-nitrophenyl α-D-galactopyranoside per min at pH 6.5 at 25 °C.

Forme physique

This product is a sterile-filtered aqueous buffered solution.

Inhibiteur

Réf. du produit
Description
Tarif

Substrat

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

K Schmid et al.
European journal of biochemistry, 67(1), 95-104 (1976-08-01)
The utilization by Escherichia coli K12 of raffinose as sole carbon source depends on a new raffinose transport system, an invertase and an alpha-galactosidase specified by the Raf-plasmid D1021. The alpha-galactosidase was purified to homogeneity from a mutant strain with
Shuo Gao et al.
Frontiers in chemistry, 9, 709581-709581 (2021-08-03)
For wide applications of the lacZ gene in cellular/molecular biology, small animal investigations, and clinical assessments, the improvement of noninvasive imaging approaches to precisely assay gene expression has garnered much attention. In this study, we investigate a novel molecular platform
Antonio Pisani et al.
Molecular genetics and metabolism, 107(3), 267-275 (2012-09-12)
Anderson-Fabry disease is an X-linked lysosomal storage disorder resulting from the deficiency of the hydrolytic enzyme alpha galactosidase A, with consequent accumulation of globotrioasoyl ceramide in cells and tissues of the body, resulting in a multi-system pathology including end organ
Aritz Pérez Ruiz de Garibay et al.
Drug design, development and therapy, 6, 303-310 (2012-11-03)
Gene-mediated enzyme replacement is a reasonable and highly promising approach for the treatment of Fabry disease (FD). The objective of the present study was to demonstrate the potential applications of solid lipid nanoparticle (SLN)-based nonviral vectors for the treatment of
Camilla Tøndel et al.
Journal of the American Society of Nephrology : JASN, 24(1), 137-148 (2013-01-01)
The effect of early-onset enzyme replacement therapy on renal morphologic features in Fabry disease is largely unknown. Here, we evaluated the effect of 5 years of treatment with agalsidase alfa or agalsidase beta in 12 consecutive patients age 7-33 years

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