Analytical Data
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Gene name
Urah
- Application
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Alternative Names
Urah；5-hydroxyisourate hydrolase
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Species
Mouse
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9CRB3
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Expression Region
1-118aa
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AA Sequence
MATESSPLTTHVLDTASGLPAQGLCLRLSRLEAPCQQWMELRTSYTNLDGRCPGLLTPSQIKPGTYKLFFDTERYWKERGQESFYPYVEVVFTITKETQKFHVPLLLSPWSYTTYRGS
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Molecular Weight
20.6 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
Urah proteins, a crucial component in the realm of biochemical research, refer to a class of proteins involved in key biological processes, including regulatory mechanisms and metabolic pathways. The study of Urah recombinant proteins has gained significant attention due to their potential applications in various fields such as medicine, biotechnology, and environmental science. These proteins can be produced in controlled laboratory settings, allowing for a better understanding of their structure and function compared to their naturally occurring counterparts. Research has shown that Urah proteins play vital roles in cellular responses and adaptations, making them interesting targets for drug development, particularly in treating diseases like cancer and metabolic disorders. Furthermore, the ability to manipulate and express these proteins through recombinant DNA technology enhances their utility in designing therapeutic agents, vaccines, and diagnostic tools. Investigations into the molecular interactions and stability of Urah proteins also pave the way for innovations in enzyme engineering and biocatalysis, contributing to greener industrial processes. Overall, the study of Urah recombinant proteins is not only pivotal for advancing our understanding of fundamental biological processes but also has far-reaching implications for the development of novel therapeutic and biotechnological applications.
