Analytical Data
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Gene name
ispU
- Application
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Alternative Names
Ditrans,polycis-undecaprenylcistransferase Undecaprenyl diphosphate synthase Short name: UDS Undecaprenyl pyrophosphate synthase Short name: UPP synthase
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Species
Escherichia coli
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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
P60472
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Expression Region
1-253aa
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Molecular Weight
32.4 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 ispU recombinant protein has garnered significant attention due to its potential implications in various fields, particularly in the understanding of bacterial pathogenesis and the development of novel therapeutic strategies. IspU, or isoprenyl diphosphate synthase, is an enzyme involved in the biosynthesis of isoprenoids, which are vital compounds for numerous physiological processes in both prokaryotic and eukaryotic organisms. Given its essential role in the mevalonate and non-mevalonate pathways, targeting IspU could provide new avenues for antimicrobial drug development, especially against resistant strains of bacteria. Additionally, the recombinant production of ispU facilitates detailed studies on its enzymatic mechanisms and substrate specificity, allowing researchers to elucidate its function in the context of cellular metabolism and stress response. Furthermore, the characterization of ispU-derived proteins can enhance our understanding of evolutionary biology and metabolic engineering, making it a pivotal focus in contemporary biochemical research. This research aims not only to explore the fundamental biological aspects of ispU but also to translate these findings into practical applications in medicine and biotechnology, showcasing the enzyme's relevance in combating infectious diseases.
