Analytical Data
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Gene name
UGPA
- Application
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Alternative Names
(UDP-glucose pyrophosphorylase)(UDPGP)(UGPase)
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Species
Musa acuminata
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9SDX3
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Expression Region
1-467aa
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Molecular Weight
58.8 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
UGPA (UDP-glucose pyrophosphorylase) is an enzyme that plays a crucial role in the synthesis of activated glucose, specifically UDP-glucose, which is a key precursor in various metabolic pathways, including glycosylation and polysaccharide biosynthesis. The study of UGPA is particularly significant due to its potential applications in biotechnology and medicine, where manipulating glycosylation processes can lead to enhanced production of therapeutic glycoproteins and improved vaccine efficacy. Understanding the structure and function of UGPA can provide insights into its regulatory mechanisms and its interaction with other metabolic enzymes. Recent advancements in molecular biology techniques and structural genomics have enabled researchers to explore the enzymatic mechanisms of UGPA at the atomic level, paving the way for the development of engineered variants with improved activity or altered substrate specificity. Additionally, the exploration of UGPA's role across different organisms highlights its evolutionary significance and potential for biotechnological exploitation across various fields, such as agriculture, where increasing resistance to pathogens through glycan modifications can be valuable. Overall, the comprehensive study of UGPA and its recombinant forms is vital in both fundamental and applied research, opening new avenues for innovation in glycan engineering and metabolic engineering.
