Analytical Data
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Gene name
UGCG
- Application
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Alternative Names
UGCG；Ceramide glucosyltransferase
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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
Q16739
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Expression Region
1-394aa
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AA Sequence
MALLDLALEGMAVFGFVLFLVLWLMHFMAIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPGYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGFAATLEQVYFGTSHPRYYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRGWRFAMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVASLIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMTIYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV
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Molecular Weight
47.7 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
UGCG (Ubiquitous Glucosylceramidase) is an enzyme that plays a crucial role in sphingolipid metabolism by catalyzing the conversion of glucosylceramide to ceramide and glucose. Research on UGCG has gained significant attention due to its implications in various pathological conditions, including Gaucher disease, cancer, and neurodegenerative disorders. The dysregulation of UGCG activity has been linked to the accumulation of glucosylceramide, which can lead to cellular toxicity and inflammation. Understanding the structure and function of UGCG, as well as the mechanisms regulating its activity, is essential for developing therapeutic strategies. Recombination of UGCG protein allows for the study of its biochemical properties and interactions in vitro, providing insights into its role in disease processes. Moreover, engineering UGCG through recombinant DNA technology holds the potential for creating novel therapies that can target glucosylceramide accumulation or modulate sphingolipid signaling pathways. Therefore, ongoing research in UGCG protein recombination aims to elucidate its biological significance and therapeutic potential, ultimately contributing to advancements in treating related metabolic disorders and enhancing our understanding of lipid metabolism.
