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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.32
MDL number:
Specific activity:
≥20 units/mg protein
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
form
buffered aqueous solution
specific activity
≥20 units/mg protein
mol wt
80 kDa
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Gene Information
Escherichia coli CFT073 ... melA(1037886)
Related Categories
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.
Physical form
This product is a sterile-filtered aqueous buffered solution.
Other Notes
One unit will hydrolyze 1 μmole of p-nitrophenyl α-D-galactopyranoside per min at pH 6.5 at 25 °C.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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
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
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
Multicomponent nanoparticles as nonviral vectors for the treatment of Fabry disease by gene therapy.
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
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