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G7163

Sigma-Aldrich

α-Galactosidase, positionally specific from Escherichia coli

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(e):

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

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About This Item

CAS-Nummer:
9025-35-8
EC-Nummer:
3.2.1.22 (BRENDA, IUBMB)
MDL-Nummer:
MFCD00130486
UNSPSC-Code:
12352204
NACRES:
NA.32

Rekombinant

expressed in E. coli

Qualitätsniveau

200

Form

buffered aqueous solution

Spezifische Aktivität

≥20 units/mg protein

Mol-Gew.

80 kDa

Versandbedingung

wet ice

Lagertemp.

2-8°C

Angaben zum Gen

Escherichia coli CFT073 ... melA(1037886)

Verwandte Kategorien

Biochem./physiol. Wirkung

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.

Einheitendefinition

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

Physikalische Form

This product is a sterile-filtered aqueous buffered solution.

Inhibitor

Produkt-Nr.
Beschreibung
Preisangaben

D9641

Deoxygalactonojirimycin hydrochloride

Substrat

Produkt-Nr.
Beschreibung
Preisangaben

Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

WGK 2

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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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
Thomas Clavel et al.
Archives of microbiology, 195(1), 43-49 (2012-10-12)
We report the characterization of one novel bacterium, strain ERD01G(T), isolated from the cecum of a TNF(deltaARE) mouse. The strain was found to belong to the genus Streptococcus based on phylogenetic analysis of partial 16S rRNA gene sequences. The bacterial
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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