Analytical Data
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Gene name
ureB
- Application
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Alternative Names
Urea amidohydrolase subunit beta
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Species
Helicobacter pylori
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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
P69996
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Expression Region
1-569aa
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Molecular Weight
65.7 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
UreB is a crucial component of the urease enzyme complex, which plays a significant role in the nitrogen cycle by catalyzing the hydrolysis of urea into ammonia and carbon dioxide. This enzyme is predominantly found in various microorganisms, including bacteria, fungi, and plants, and facilitates the utilization of urea as a nitrogen source. The study of UreB recombinant protein has gained prominence due to its potential applications in biotechnology and agriculture, as urease can improve soil fertility and assist in bioremediation processes. Moreover, understanding the molecular structure and function of UreB can provide insights into enzyme mechanisms, and its inhibition can be explored for therapeutic targets in managing urease-related disorders. Research has focused on gene cloning, protein expression, and characterization of UreB to facilitate the development of biosensors and biocatalysts. Furthermore, with increasing interest in sustainable agriculture and environmental management, engineered ureases may offer eco-friendly alternatives to conventional fertilizers and chemical treatments. As such, the exploration of UreB's properties and applications is crucial not only for enhancing agricultural productivity but also for addressing environmental challenges.
