Analytical Data
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Gene name
GALE
- Application
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Alternative Names
GALE;UDP-glucose 4-epimerase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14376
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Expression Region
1-348aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAEKVLVTGGAGYIGSHTVLELLEAGYLPV VIDNFHNAFRGGGSLPESLRRVQELTGRSVEFEEMDILDQGALQRLFKKY SFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMKAHGVKNLVFS SSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKTWNA VLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDY DTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQM VQAMEKASGKKIPYKVVARREGDVAACYANPSLAQEELGWTAALGLDRMC EDLWRWQKQNPSGFGTQA
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Molecular Weight
40 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
GALE (UDP-galactose 4-epimerase) is a crucial enzyme in the galactose metabolism pathway, responsible for catalyzing the interconversion of UDP-galactose and UDP-glucose. Deficiency in GALE activity can lead to disorders such as galactosemia, characterized by an inability to properly metabolize galactose, resulting in serious health complications such as liver damage, cognitive impairment, and developmental delays. Research into GALE recombinant proteins has gained momentum due to their potential applications in gene therapy, biotechnology, and metabolic engineering. By producing functional GALE proteins through recombinant DNA technology, researchers can delve into enzyme kinetics, structure-function relationships, and potential therapeutic interventions for metabolic disorders. Additionally, understanding GALE’s structure through techniques such as X-ray crystallography and NMR spectroscopy has provided insights into substrate specificity and regulatory mechanisms. Enhanced characterization of GALE not only aids in the development of treatments for galactosemia but also contributes to the broader understanding of carbohydrate metabolism, enabling advancements in dietary supplements and interventions for microbial production of galactose-derived compounds. The exploration of GALE recombinant proteins thus holds significant promise for both fundamental biological research and clinical applications.
