Analytical Data
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Gene name
oprP
- Application
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Alternative Names
Outer membrane protein D1
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Species
Pseudomonas aeruginosa
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05695
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Expression Region
30-440aa
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Molecular Weight
61.2 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
OprP is a porin protein found in the outer membrane of Pseudomonas aeruginosa, an opportunistic pathogen known for its resistance to multiple antibiotics. This protein plays a critical role in the transport of small molecules, such as phosphate and some antibiotics, across the bacterial membrane, thereby influencing the bacterium's growth, virulence, and drug susceptibility. The study of OprP and its recombinant forms has gained significance due to the increasing prevalence of multidrug-resistant strains of P. aeruginosa, which pose a significant threat in clinical settings, particularly for immunocompromised patients. Understanding the structure and function of OprP can provide insights into its mechanisms of action and interaction with various substrates, which may lead to the identification of novel therapeutic targets. Research has focused on the characterization of OprP’s molecular structure, its transport dynamics, and its role in biofilm formation—a key factor in the pathogenesis of P. aeruginosa infections. Moreover, recombinant OprP can serve as a valuable tool for studying porin function and for developing new strategies to combat bacterial infections. The ongoing investigation into OprP aims to elucidate its potential as a target for drug design and to enhance our overall understanding of bacterial membrane transport processes.
