Saltar al contenido
Merck
Todas las fotos(1)

Key Documents

View All Documentation

G7163

Sigma-Aldrich

α-Galactosidase, positionally specific from Escherichia coli

recombinant, expressed in E. coli, buffered aqueous solution

Sinónimos:

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

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización
Todas las fotos(1)

About This Item

Número de CAS:
9025-35-8
Comisión internacional de enzimas:
3.2.1.22 (BRENDA, IUBMB)
MDL number:
MFCD00130486
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

Quality Level

200

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)

Categorías relacionadas

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

Referencia del producto
Descripción
Precios

D9641

Deoxygalactonojirimycin hydrochloride

substrate

Referencia del producto
Descripción
Precios

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

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
Romain Merceron et al.
The Journal of biological chemistry, 287(47), 39642-39652 (2012-09-27)
The α-galactosidase AgaA from the thermophilic microorganism Geobacillus stearothermophilus has great industrial potential because it is fully active at 338 K against raffinose and can increase the yield of manufactured sucrose. AgaB has lower affinity for its natural substrates but
Hongwei Gao et al.
Artificial cells, nanomedicine, and biotechnology, 41(1), 32-36 (2012-10-04)
Enzymatical conversion of A or B RBCs into group O RBCs (ECORBCs) was achieved by using α-N-acetylgalactosaminidase and α-galactosidase, respectively. Now, we initiated AB to O-RBC conversion by using these two enzymes together. But α-N-acetylgalactosaminidase and α-galactosidase's preserving and their
Dominique P Germain et al.
Orphanet journal of rare diseases, 7, 91-91 (2012-11-28)
Fabry disease (FD) is a genetic disorder resulting from deficiency of the lysosomal enzyme α-galactosidase A (α-Gal A), which leads to globotriaosylceramide (GL-3) accumulation in multiple tissues. We report on the safety and pharmacodynamics of migalastat hydrochloride, an investigational pharmacological
Costanza Simoncini et al.
The neurologist, 18(6), 413-414 (2012-11-02)
Fabry disease (FD) is a rare, X-linked lysosomal storage disorder with multiorgan involvement. FD is caused by a partial or total deficit of α-galactosidase A enzyme, which is responsible for the accumulation of glycosphingolipids in a variety of cell types.
Ver todos los artículos relacionados

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico