Analytical Data
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Gene name
UGGT1
- Application
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Alternative Names
UGTR; HUGT1; GT; UGCGL1; UGGT; UGT1; UDP-glucose ceramide glucosyltransferase-like 1
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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
Q9NYU2
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Expression Region
Leu1221~Leu1536
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Molecular Weight
41kDa
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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
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Protein Description
UGGT1 (UDP-glucose:glycoprotein glucosyltransferase 1) is an enzyme that plays a crucial role in the quality control of glycoprotein folding within the endoplasmic reticulum (ER). It recognizes misfolded glycoproteins and tags them with glucose residues, allowing them to be retrained within the ER for proper folding or directing them for degradation if they fail to achieve the correct conformation. Given its pivotal role in glycoprotein maturation and the maintenance of cellular homeostasis, UGGT1 has garnered interest in various fields, including molecular biology, biochemistry, and pharmaceuticals. Deficiencies or malfunctions in this enzyme have been linked to a range of diseases, such as congenital disorders of glycosylation and various neurodegenerative diseases, highlighting its importance in human health. Studies involving recombinant UGGT1 proteins have led to a deeper understanding of its enzymatic function, substrate specificity, and interaction with other chaperone proteins. Furthermore, producing UGGT1 as a recombinant protein opens avenues for therapeutic interventions and the development of robust biotechnological applications, including enhancing protein yield and functionality during biomanufacturing processes. Thus, research into UGGT1 recombinant protein is not only fundamental for advancing our understanding of glycoprotein biogenesis but also holds significant potential for therapeutic and industrial applications.
