Analytical Data
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Gene name
oprF
- Application
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Alternative Names
oprF；Outer membrane porin 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
P13794
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Expression Region
25-350aa
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AA Sequence
QGQNSVEIEAFGKRYFTDSVRNMKNADLYGGSIGYFLTDDVELALSYGEYHDVRGTYETGNKKVHGNLTSLDAIYHFGTPGVGLRPYVSAGLAHQNITNINSDSQGRQQMTMANIGAGLKYYFTENFFAKASLDGQYGLEKRDNGHQGEWMAGLGVGFNFGGSKAAPAPEPVADVCSDSDNDGVCDNVDKCPDTPANVTVDANGCPAVAEVVRVQLDVKFDFDKSKVKENSYADIKNLADFMKQYPSTSTTVEGHTDSVGTDAYNQKLSERRANAVRDVLVNEYGVEGGRVNAVGYGESRPVADNATAEGRAINRRVEAEVEAEAK
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Molecular Weight
44.1 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
OprF is a prominent outer membrane protein found in Pseudomonas aeruginosa, a bacterium known for its role in nosocomial infections and its antibiotic resistance. Research on OprF has gained momentum due to its potential applications in vaccine development and protein engineering. The protein functions as a porin, facilitating the transport of small molecules across the bacterial membrane, and it is also involved in virulence and immune evasion. Understanding OprF's structure and function is crucial for deciphering the mechanisms of P. aeruginosa pathogenicity and can lead to innovative strategies to combat infections caused by this pathogen. Recombinant OprF, produced through synthetic biology techniques, serves as a valuable tool for studying the protein's properties and interactions with host immune systems. Additionally, its immunogenic potential has been explored to gauge its effectiveness as a vaccine candidate. Research efforts are focused on optimizing expression systems for high yields of functional OprF, examining its antigenic characteristics, and assessing its role in eliciting protective immune responses. Overall, the study of recombinant OprF is not only significant for understanding the biology of Pseudomonas aeruginosa but also holds promise for therapeutic advancements against antibiotic-resistant infections.
