Analytical Data
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Gene name
pfo
- Application
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Alternative Names
Theta-toxin Thiol-activated cytolysin
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Species
Clostridium perfringens
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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
P0C2E9
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Expression Region
29-500aa
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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
Related Products
Protein Description
The research on PFO (perfringolysin O) recombinant protein has gained significant attention due to its potential applications in various fields, including medical diagnostics, therapeutics, and biotechnology. PFO is a pore-forming toxin produced by the bacterium Clostridium perfringens, and it plays a crucial role in pathogenicity by disrupting cellular membranes. Understanding the structure and function of PFO at the molecular level can provide valuable insights into its mechanisms of action and how it can be utilized or inhibited. In recent years, advances in recombinant DNA technology have made it possible to produce PFO in a laboratory setting, allowing researchers to study its properties in detail without the complications associated with working directly with the pathogenic bacterium. Additionally, PFO has been explored as a molecular tool for targeted drug delivery and as a component in vaccine development, given its ability to form pores in lipid membranes that can be harnessed for therapeutic purposes. The ability to manipulate PFO through recombinant techniques opens new avenues for enhancing its efficacy and safety in biomedical applications, making it a promising candidate for further investigation in the realms of immunology and molecular therapy. Moreover, ongoing research aims to delineate the functional domains of PFO and to develop modified versions with improved biocompatibility and specificity, thereby expanding its utility in various scientific and clinical applications.
