Analytical Data
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Gene name
pagC
- Application
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Alternative Names
pagC；Virulence membrane Protein PagC
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Species
Erwinia
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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
D2T690
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Expression Region
24-185aa
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AA Sequence
DSHALSIGYAQSRVQDFKNLRGVNLKYRYEPNSLLGVITSFSYMSAGGHEFDSLSWGDTYYDDRIKVKYYSLLIGPSYRINKYVSLYAVSGLGSSKLDLTQNYRHTNYTYTEHTASNTTSFAYGAGVQINPLKNIAIDISYEKSKINAKKINGFSMGIGYHF
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Molecular Weight
25.7 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
PagC is a virulence factor associated with the pathogenicity of Yersinia pestis, the bacterium responsible for the plague. This protein plays a key role in the bacterium's ability to evade the host's immune response, particularly by aiding in the formation of a protective capsule. The understanding of PagC is crucial for developing new therapeutic strategies against plague infections. Research on PagC has focused on its structure and function, revealing insights into how it interacts with host cells and contributes to the bacterium's survival in hostile environments. Additionally, studies have explored the recombinant expression of PagC to analyze its properties and potential applications in vaccine development. Investigating PagC through recombinant protein technologies allows researchers to create safer and more effective vaccines by utilizing non-pathogenic systems for antigen production. This line of research not only enhances our understanding of Yersinia pestis's virulence mechanisms but also contributes to broader efforts in infectious disease control and prevention. As antimicrobial resistance rises worldwide, elucidating the role of PagC in host-pathogen interactions represents a strategic focus in the development of novel therapeutic interventions.
