Recombinant Human UDP-Glucose 4-Epimerase/GALE is produced by our E. coli expression system. The target protein is expressed with sequence (Met1-Ala348) of Human GALE fused with a His tag at the N-terminus.
Reinheit
> 95 % as determined by reducing SDS-PAGE.
Sterilität
0.2 μm filtered
Endotoxin-Niveau
Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
GALE
Spezies: Human
Wirt: Tobacco (Nicotiana tabacum)
Recombinant
>80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
ELISA, SDS, WB
GALE
Spezies: Maus
Wirt: Tobacco (Nicotiana tabacum)
Recombinant
≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
ELISA, SDS, WB
GALE
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
> 80 % as determined by SDS-PAGE and Coomassie blue staining
AbP, STD
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Rekonstitution
It is not recommended to reconstitute to a concentration less than 100 μg/mL. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Buffer
Supplied as a 0.2 μm filtered solution of 50 mM TrisHCl, 150 mM NaCl, 2 mM DTT, 1 mM EDTA, pH 8.0.
Konservierungsmittel
Dithiothreitol (DTT)
Vorsichtsmaßnahmen
This product contains Dithiothreitol (DTT): a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handhabung
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
Lagerung
-80 °C
Informationen zur Lagerung
Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
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Sub Type
Fusionprotein
Hintergrund
The enzyme UDP-Glucose 4-Epimerase (GALE) is a homodimeric epimerase found in bacterial, plant and mammalian cells. UDP-Glucose 4-Epimerase performs the final step in the Leloir pathway of Galactose metabolism, it catalyzes two distinct but analogous reactions: the epimerization of UDP-Gglucose to UDP-Galactose and the epimerization of UDP-N-Acetylglucosamine to UDP-N-Acetylgalactosamine. The bifunctional nature of the enzyme has the important metabolic consequence that mutant cells (or individuals) are dependent not only on exogenous galactose, but also on exogenous N-acetylgalactosamine as a necessary precursor for the synthesis of glycoproteins and glycolipids. Alternative Names: UDP-Glucose 4-Epimerase, Galactowaldenase, UDP-Galactose 4-Epimerase, GALE