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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

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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»

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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
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
Xiao-Liang Pan et al.
The journal of physical chemistry. B, 117(2), 484-489 (2012-12-20)
The enzyme α-galactosidase (α-GAL), a member of glycoside hydrolase family 27, catalyzes the removal of a nonreducing terminal α-galactose residue from polysaccharides, glycolipids, and glycopeptides. α-GAL is believed to have the double displacement retaining reaction mechanism. In this work, the
M Benelmekki et al.
Colloids and surfaces. B, Biointerfaces, 101, 370-375 (2012-09-27)
Biomagnetic immobilization of histidine-rich proteins based on the single-step affinity adsorption of transition metal ions continues to be a suitable practice as a cost effective and a up scaled alternative to the to multiple-step chromatographic separations. In our previous work
Junpei Zhou et al.
Journal of microbiology and biotechnology, 22(11), 1532-1539 (2012-11-06)
The α-galactosidase-coding gene agaAJB13 was cloned from Sphingomonas sp. JB13 showing 16S rDNA (1,343 bp) identities of < or =97.2% with other identified Sphingomonas strains. agaAJB13 (2,217 bp; 64.9% GC content) encodes a 738-residue polypeptide (AgaAJB13) with a calculated mass
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