Recombinant Human UDP-Glucose 4-Epimerase/GALE (N-6His)
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| Amount : | 50 µg |
| Content : | Supplied as a 0.2 µm filtered solution of 50mM TrisHCl, 150mM NaCl, 2mM DTT, 1mM EDTA, pH 8.0. |
| Storage condition : | Store at -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles. |
| AA sequence : | MGSSHHHHHHSSGLVPRGSHMAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRRVQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKTWNAVLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGTQA |
Source: E.coli.
MW :40.44kD.
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. 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.
MW :40.44kD.
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. 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.
Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| BioGrid: | 108855. 23 interactions. |
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