Recombinant Human UDP-Glucose 4-Epimerase/GALE
| Product name: | Recombinant Human UDP-Glucose 4-Epimerase/GALE | 
| Source: | E.coli | 
| Purity: | Greater than 95% as determined by reducing SDS-PAGE. | 
| Buffer Formulation: | Supplied as a 0.2 μm filtered solution of 50mM TrisHCl, 150mM NaCl, 2mM DTT, 1mM EDTA, pH 8.0. | 
| Applications: | Applications:SDS-PAGE; WB; ELISA; IP. | 
| Storage: | Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months. | 
| UOM: | 100ug/50ug/200ug/1mg/1g | 
| Source | E.coli | 
| Description | Recombinant Human GALE is produced by our E.coli expression system and the target gene encoding Met1-Ala348 is expressed with a 6His tag at the N-terminus. | 
| Names | UDP-Glucose 4-Epimerase, Galactowaldenase, UDP-Galactose 4-Epimerase, GALE | 
| Accession # | Q14376 | 
| Formulation | Supplied as a 0.2 μm filtered solution of 50mM TrisHCl, 150mM NaCl, 2mM DTT, 1mM EDTA, pH 8.0. | 
| Shipping | The product is shipped on dry ice/ice packs. | 
| Storage | Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles. | 
| Purity | Greater than 95% as determined by reducing SDS-PAGE. | 
| Endotoxin | Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test. | 
| Amino Acid Sequence | 
					MGSSHHHHHHSSGLVPRGSHMAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSL PESLRRVQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKPLDYYRVNLT GTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQAD KTWNAVLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRD YIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVA ACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGTQA
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| Background | 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. | 


 


 
              








