Analytical Data
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Gene name
uspF
- Application
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Alternative Names
uspF；ynaF；yzzL；Universal stress Protein F
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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
P37903
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Expression Region
1-144aa
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AA Sequence
MNRTILVPIDISDSELTQRVISHVEEEAKIDDAEVHFLTVIPSLPYYASLGLAYSAELPAMDDLKAEAKSQLEEIIKKFKLPTDRVHVHVEEGSPKDRILELAKKIPAHMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR
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Molecular Weight
32.0 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
Related Products
Protein Description
The study of the uspF recombinant protein is rooted in the growing interest in understanding the function of universal stress proteins (USPs) in response to environmental stress conditions in bacteria. USPs play a crucial role in enabling microorganisms to adapt to various stresses, including oxidative stress, nutrient deprivation, and other unfavorable conditions. The uspF gene, which encodes a member of this protein family, is of particular interest due to its potential involvement in bacterial survival and pathogenicity. Research has indicated that uspF is upregulated in response to stress, suggesting it may have a protective role in maintaining cellular integrity. By examining the recombinant form of the uspF protein, scientists aim to elucidate its structure and biochemical properties, which could shed light on its specific functions and mechanisms of action. This research not only contributes to the fundamental understanding of bacterial stress responses but may also have implications for developing novel antibacterial strategies, as targeting such stress response pathways could hinder the survival of pathogenic bacteria under stress conditions. Consequently, investigations into the uspF protein can provide insights into microbial resilience, with potential applications in medical microbiology and biotechnology.
