Analytical Data
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Gene name
pfo
- Application
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Alternative Names
pfo；pfoA；pfoR；Perfringolysin O
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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
P0C2E9
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Expression Region
29-500aa
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AA Sequence
KDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN
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Molecular Weight
68.7 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
PFO (Perfringolysin O) is a pore-forming toxin derived from the bacterium Clostridium perfringens, which has garnered significant attention in biomedical research due to its unique structural and functional properties. Initially studied for its role in pathogenesis, PFO has been recognized for its potential applications in various fields, including immunology and drug delivery. Researchers have focused on the recombinant expression of PFO to facilitate studies on its mechanism of action, as well as to explore its utility as a vaccine adjuvant and a tool for targeted drug delivery. By generating recombinant PFO, scientists can investigate its interactions with cellular membranes, its ability to stimulate immune responses, and its properties as a therapeutic agent. Studies have shown that modified versions of PFO can enhance the efficacy of vaccines by promoting a stronger immune response. Moreover, its specificity for certain cell types opens avenues for developing targeted therapies for diseases characterized by specific cellular markers. Overall, the recombinant PFO research represents a promising frontier in biotechnology, combining insights from microbial pathogenesis with innovative therapeutic strategies.
