Analytical Data
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Gene name
porA
- Application
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Alternative Names
porA；PVS；Poliovirus receptor
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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
P0DH58
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Expression Region
20-392aa
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AA Sequence
DVSLYGEIKAGVEGRNYQLQLTEAQAANGGASGQVKVTKVTKAKSRIRTKISDFGSFIGFKGSEDLGDGLKAVWQLEQDVSVAGGGATQWGNRESFIGLAGEFGTLRAGRVANQFDDASQAIDPWDSNNDVASQLGIFKRHDDMPVSVRYDSPEFSGFSGSVQFVPIQNSKSAYTPAYYTKNTNNNLTLVPAVVGKPGSDVYYAGLNYKNGGFAGNYAFKYARHANVGRNAFELFLIGSGSDQAKGTDPLKNHQVHRLTGGYEEGGLNLALAAQLDLSENGDKTKNSTTEIAATASYRFGNAVPRISYAHGFDFIERGKKGENTSYDQIIAGVDYDFSKRTSAIVSGAWLKRNTGIGNYTQINAASVGLRHKF
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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
PorA is a key surface protein found in various pathogenic bacteria, particularly in Neisseria species, where it plays a crucial role in immune evasion and bacterial virulence. The study of PorA recombinant proteins has gained significant interest due to their potential applications in vaccine development and diagnostics. Understanding the structure-function relationship of PorA is critical, as it may provide insights into how these proteins interact with host immune systems. Research has demonstrated that PorA can elicit robust immunogenic responses, making it a candidate for inclusion in multivalent vaccines aimed at combating bacterial infections. Furthermore, the production of PorA as a recombinant protein allows for detailed studies of its properties and interactions, facilitating the development of novel therapeutic strategies. The advancement of recombinant DNA technology has enabled researchers to produce PorA in sufficient quantities, leading to a better understanding of its antigenic characteristics and potential protective efficacy. As antibiotic resistance becomes an escalating concern, the exploration of recombinant PorA in various contexts, such as vaccine formulation and therapeutic intervention, is timely and essential. Thus, ongoing research into PorA recombinant proteins not only enhances our understanding of bacterial pathogenesis but also paves the way for innovative approaches to prevent and treat bacterial infections.
