Analytical Data
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Gene name
UGGT2
- Application
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Alternative Names
HUGT2; UGCGL2; UGT2; UDP-glucose ceramide glucosyltransferase-like 1
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Species
Human
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NYU1
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Expression Region
His1221~Arg1408
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Molecular Weight
29kDa
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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
UGGT2 (UDP-glucose: glycoprotein glucosyltransferase 2) is an essential enzyme involved in the quality control of glycoprotein folding in the endoplasmic reticulum (ER). It plays a critical role in the glycoprotein maturation process by transferring glucose residues to improperly folded glycoproteins, which serves as a signal for their retention in the ER and eventual refolding or degradation through the ER-associated degradation (ERAD) pathway. The study of UGGT2 is particularly relevant given the increasing recognition of the importance of glycosylation in protein function and its implications in various diseases, including cancer and neurodegenerative disorders. Researchers have also shown that UGGT2 is involved in the viral life cycle of several pathogens, affecting their virulence and host immune responses, which highlights its potential as a therapeutic target. With advancements in recombinant DNA technology, scientists are now able to produce UGGT2 as a recombinant protein for structural and functional analyses. This allows for a deeper understanding of its enzymatic mechanisms, substrate specificities, and interactions with other cellular components. The ongoing research into UGGT2 not only enhances our comprehension of protein folding and modification but also paves the way for the development of novel strategies aimed at modulating glycoprotein functions for therapeutic interventions.
