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G7163

Sigma-Aldrich

α-Galactosidase, positionally specific from Escherichia coli

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

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

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About This Item

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

recombinant

expressed in E. coli

Quality Level

form

buffered aqueous solution

specific activity

≥20 units/mg protein

mol wt

80 kDa

shipped in

wet ice

storage temp.

2-8°C

Gene Information

Escherichia coli CFT073 ... melA(1037886)

Biochem/physiol Actions

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.

Unit Definition

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

Physical form

This product is a sterile-filtered aqueous buffered solution.

inhibitor

Product No.
Description
Pricing

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
Takura Wakinaka et al.
Glycobiology, 23(2), 232-240 (2012-10-24)
Bifidobacterium bifidum is one of the most frequently found bifidobacteria in the intestines of newborn infants. We previously reported that B. bifidum possesses unique metabolic pathways for O-linked glycans on gastrointestinal mucin (Yoshida E, Sakurama H, Kiyohara M, Nakajima M

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