Analytical Data
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Gene name
UPP1
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简介
UPP1 protein is a key member of the PNP/UDP phosphorylase family and plays an important role in cellular processes, especially nucleotide metabolism. UPP1 shares conserved features with related proteins and is involved in phosphorylase activity. UPP1 Protein, Human (His) is the recombinant human-derived UPP1 protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
UPP1 Protein; Uridine Phosphorylase 1; UPP1
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86Y75
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Expression Region
M1-A173
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Protein Length
Full Length
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Molecular Weight
21 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
UPP1, or uridine phosphorylase 1, is an enzyme that plays a crucial role in nucleoside metabolism, specifically in the salvage pathway of uridine recycling. Its primary function is to catalyze the phosphorolytic cleavage of uridine, producing uracil and ribose-1-phosphate, which are vital for nucleotide synthesis and cellular energy metabolism. Research on UPP1 has gained significant interest due to its potential implications in various physiological and pathological processes, including cancer, neurodegenerative diseases, and metabolic disorders. Understanding the structure and function of UPP1 is essential for identifying therapeutic targets and developing inhibitors that could modulate its activity for clinical benefits. Recombinant UPP1 protein expression and purification have become key approaches in studying this enzyme's biochemical properties, substrate specificity, and regulatory mechanisms. By utilizing advanced techniques such as molecular cloning, expression in bacterial or eukaryotic systems, and subsequent characterization through assays and structural biology methods, researchers aim to gain insights into UPP1's role in health and disease. Additionally, elucidating the enzyme's interactions with other biomolecules can provide deeper knowledge of its biological significance and therapeutic potential. In summary, UPP1 represents a promising target for drug discovery and therapeutic interventions, making its recombinant protein research a vital area of investigation in the field of biochemistry and molecular biology.











