Analytical Data
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Gene name
rpsO
- Application
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Alternative Names
rpsO; secC; b3165; JW3134; 30S ribosomal protein S15; Small ribosomal subunit protein uS15
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Species
Escherichia coli
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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
P0ADZ4
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Expression Region
2-89aa
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Molecular Weight
14.1 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
RpsO, a ribosomal protein found in bacteria, is part of the 30S ribosomal subunit and plays a crucial role in protein synthesis. Research on RpsO has gained prominence due to its essential function in ribosome assembly and stability, which impacts the overall efficiency of translation. Understanding the structure and function of RpsO is vital for elucidating the mechanisms of ribosome biogenesis and the interactions between ribosomal proteins and ribosomal RNA. Moreover, RpsO has been investigated for its potential applications in antibiotic development, as targeting ribosomal proteins can hinder bacterial growth and survival. Given the rising prevalence of antibiotic resistance, studying RpsO could lead to novel therapeutic strategies. Recombinant RpsO proteins have been produced to facilitate in-depth structural and functional analyses, enabling researchers to explore its interactions within the ribosomal complex and its role in the translation process. This research not only enhances our understanding of bacterial ribosome function but also contributes to the broader field of molecular biology and the discovery of new antimicrobial agents. Thus, RpsO serves as a promising target for both fundamental research and practical applications in combating bacterial infections.
