Analytical Data
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Gene name
porA
- Application
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Alternative Names
Class 1 protein
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Species
Neisseria meningitidis serogroup B
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0DH58
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Expression Region
20-392aa
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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
Related Products
Protein Description
PorA, an outer membrane protein found in Neisseria meningitidis, plays a crucial role in the virulence and immunogenicity of this pathogenic bacterium. As a vital component of the bacterial surface, PorA is known to be involved in immune evasion by modulating the host's immune response. Its variable regions provide antigenic diversity, which allows N. meningitidis to evade host defenses, posing challenges for vaccine development. Research on recombinant PorA proteins aims to elucidate their structural and functional properties, enabling the design of effective vaccines and diagnostic tools. Studies have demonstrated that recombinant PorA can induce a robust immune response in hosts, highlighting its potential as a vaccine candidate. Furthermore, investigating the immunogenicity of different PorA variants can provide insights into the adaptive mechanisms of this pathogen and lead to the development of broad-spectrum vaccines that can effectively target multiple strains. As antibiotic resistance continues to rise, understanding the immunological implications of PorA is vital for advancing public health strategies against meningococcal disease. Hence, the exploration of recombinant PorA proteins not only enhances our understanding of bacterial pathogenesis but also paves the way for innovative approaches to combat infectious diseases.
