Analytical Data
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Gene name
UGT8
- Application
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Alternative Names
CGT; Cerebroside synthase; UDP-Galactose Ceramide Galactosyltransferase; 2-Hydroxyacylsphingosine 1-Beta-Galactosyltransferase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16880
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Expression Region
Gly198~Lys541
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Molecular Weight
44kDa
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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
UGT8 (UDP-Glucuronosyltransferase 8) is an important enzyme involved in the biosynthesis of myelin and the metabolism of various substrates, including lipids, hormones, and drugs. As a member of the UDP-glucuronosyltransferase family, UGT8 catalyzes the transfer of glucuronic acid to acceptor molecules, which facilitates their excretion and enhances their solubility. The enzyme plays a critical role in the process of glycosylation, especially in the modification of glycosphingolipids, which are essential components of myelin sheaths in the nervous system. Dysfunction or mutations in the UGT8 gene are associated with several neurological disorders, such as Krabbe disease and other myelin-related pathologies. Therefore, studying the recombinant UGT8 protein is vital for understanding its biochemical role, regulatory mechanisms, and potential therapeutic applications. The production of UGT8 as a recombinant protein allows researchers to investigate its enzymatic activity, substrate specificity, and interaction with other biomolecules in vitro. This research not only sheds light on the fundamental processes underlying lipid metabolism and myelination but also opens avenues for the development of targeted treatments for conditions linked to UGT8 deficiencies. Furthermore, insights gained from these studies may ultimately contribute to advancements in regenerative medicine and neuroprotection strategies in the context of demyelinating disorders. Thus, the research on UGT8 recombinant protein serves a pivotal role in both basic science and applied medical fields, highlighting its significance in neurobiology and pharmacology.
