Analytical Data
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Gene name
uox
- Application
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Alternative Names
uox；Uricase
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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
P25688
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Expression Region
2-303aa
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AA Sequence
AHYHDNYGKNDEVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLRSKKDYLHGDNSDIIPTDTIKNTVHVLAKLRGIRNIETFAMNICEHFLSSFNHVTRAHVYVEEVPWKRFEKNGIKHVHAFIHTPTGTHFCEVEQMRNGPPVIHSGIKDLKVLKTTQSGFEGFLKDQFTTLPEVKDRCFATQVYCKWRYQRRDVDFEAIWGAVRDIVLQKFAGPYDKGEYSPSVQKTLYDIQVLSLSQLPEIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVKRKLPSRL
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Molecular Weight
41.8 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
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Protein Description
Uox, or urate oxidase, is an enzyme that catalyzes the oxidation of uric acid to allantoin, playing a crucial role in the purine metabolism pathway. Its significance in biomedical research arises from its potential therapeutic applications in hyperuricemia and gout, conditions characterized by elevated uric acid levels in the blood. In recent years, there has been growing interest in the recombinant production of Uox to develop novel treatments. Traditionally, Uox was derived from animal sources, but concerns regarding purity, safety, and ethical considerations have driven researchers to explore microbial expression systems for producing recombinant Uox. This approach not only enhances yield and scalability but also allows for better control over post-translational modifications. Furthermore, the advancement of molecular biology techniques has enabled the optimization of Uox for improved enzymatic activity and stability. Studies have shown that recombinant Uox can effectively lower uric acid levels in animal models, offering a promising strategy for treating gout and other related disorders. As research progresses, understanding the structure-function relationship of Uox and optimizing its properties through genetic engineering will be paramount in developing a safe, effective, and sustainable biosynthetic alternative for managing hyperuricemia.
