Analytical Data
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Gene name
uvsE
- Application
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Alternative Names
uvsE；UV DNA damage endonuclease
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Species
E.coli
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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
B7IR00
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Expression Region
1-317aa
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AA Sequence
MIMRFGYVSHAMALWDCSPAKTMTFTSFKKLSKQEREDKLYHVIRQNLEHTIRILHYNIAHEIPLYRLSSSIVPLATHPEVEFDYIGVFTPLWRKIGALIKEHNLRISFHPNQFTLFTSDKPHITTNAITDMTYHYKILDAIGIADSSYINIHVGGAYGNKEKAIERFHENIKKLPAHIKKQMTLENDDKTYTTSETLSICQKENIPFVFDYHHHMANLCEQPLEELLPAIFETWSHTNISPKVHISSPRSEKEFRAHAEYIDLEFIKPFLHVAKKNNHNFDIMIESKQKDLALFRLIDELSAIRGIKRISGAMLQW
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Molecular Weight
44.0 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
The study of the uvse recombinant protein is rooted in the broader context of understanding virus-host interactions, particularly in the field of virology and biotechnology. Uvse, a protein derived from certain viral or microbial sources, plays a crucial role in the life cycle of its producing organism, often facilitating processes like replication, assembly, or immune evasion. Researchers are increasingly focusing on uvse because of its potential applications in developing novel antiviral therapies, vaccines, and diagnostic tools. Furthermore, the recombinant expression of uvse allows for in-depth analysis of its structure and function, providing insights into its mechanism of action and interactions with host cells. By utilizing techniques such as molecular cloning and protein purification, scientists can produce large quantities of uvse in a controlled laboratory environment, enabling comprehensive studies that contribute to our understanding of viral pathogenesis and the development of strategies to combat viral infections. As the global threat of emerging viral diseases continues to rise, the exploration of uvse and its properties has become an essential area of research, promising advancements in therapeutic interventions and enhancing our preparedness against future outbreaks.
