Analytical Data
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Gene name
pyrE
- Application
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Alternative Names
Short name:OPRT Short name:OPRTase
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Species
Laribacter hongkongensis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
C1D6F5
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Expression Region
1-213aa
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Molecular Weight
38.9 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
The study of pyrE recombinant protein is rooted in its significant role in the biosynthesis of pyrimidine nucleotides, which are essential for DNA and RNA synthesis in all living organisms. PyrE, a gene found in various microorganisms, encodes a protein involved in the salvage pathway for pyrimidine nucleotide synthesis, particularly in the recovery of uracil. This pathway is crucial for maintaining adequate levels of nucleotides, especially under conditions where de novo synthesis is insufficient. Research on pyrE and its recombinant protein has gained attention for its potential applications in biotechnology and medicine. Understanding the structure and function of pyrE can provide insights into metabolic engineering, enzyme activity, and the development of new therapeutic strategies, including antimicrobial agents. Furthermore, as antimicrobial resistance becomes an increasing global concern, exploring microbial pathways such as those involving pyrE could lead to innovative approaches for drug development. Overall, the investigation of pyrE recombinant protein not only enhances our knowledge of microbial metabolism but also opens avenues for practical applications in health and industry.
