Analytical Data
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Gene name
prn
- Application
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Alternative Names
P.93
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Species
Bordetella pertussis
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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
P14283
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Expression Region
632-910aa
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Molecular Weight
45.8 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
PRN recombinant proteins, derived from the "PRN" (Pertactin) gene of Bordetella pertussis, have gained attention in immunological and vaccine research due to their potential applications in the development of effective vaccines against respiratory infections. Pertactin is an important adhesin that plays a crucial role in the pathogenicity of B. pertussis, the bacterium responsible for whooping cough. As the incidence of this disease has resurged in many regions, there is an urgent need for improved vaccination strategies that can provide better and longer-lasting immunity. Researchers have focused on the production and characterization of PRN recombinant proteins to explore their immunogenic properties. These proteins can be utilized as vaccine candidates, either alone or in combination with other antigens, to enhance the immune response against B. pertussis. Furthermore, studying the structure-function relationship of PRN recombinant proteins may offer insights into designing more effective vaccines and therapeutics. The use of recombinant DNA technology allows for the efficient production of these proteins in various expression systems, facilitating large-scale production and extensive preclinical studies. Overall, the research on PRN recombinant proteins represents a promising avenue for advancing our understanding of Bordetella pertussis infection and improving public health outcomes through enhanced vaccine development.
