Analytical Data
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Gene name
oprI
- Application
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Alternative Names
oprI；Major outer membrane lipoProtein
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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
P11221
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Expression Region
1-83aa
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AA Sequence
MNNVLKFSALALAAVLATGCSSHSKETEARLTATEDAAARAQARADEAYRKADEALGAAQKAQQTADEANERALRMLEKASRK
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Molecular Weight
40.3 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 OprI protein, a key outer membrane lipoprotein found in Pseudomonas aeruginosa, has attracted significant attention in research due to its critical role in bacterial pathogenesis and its potential as a vaccine target. As a major component of the bacterial outer membrane, OprI is involved in various vital processes, including nutrient uptake, antibiotic resistance, and immune evasion. Its unique structural properties allow for interactions with host cells, which facilitate infection. Understanding the biochemical and structural characteristics of OprI can provide insights into its mechanisms of action and reveal potential strategies for therapeutic intervention. With the rise of multidrug-resistant strains of P. aeruginosa, there is an urgent need for novel treatment approaches, making OprI a focal point for vaccine development and drug discovery efforts. Researchers are investigating recombinant OprI protein for its immunogenic properties, aiming to induce protective immune responses against P. aeruginosa. The knowledge gained from studying OprI can significantly contribute to the development of effective vaccines and enhance our understanding of bacterial pathogenesis, thereby addressing the global health challenge posed by antibiotic-resistant infections.
