Analytical Data
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Gene name
vlpE
- Application
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Alternative Names
vlpE；Variant surface antigen E
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Species
Mycoplasma
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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
Q49537
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Expression Region
30-243aa
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AA Sequence
CGQTTDNLSQSQQPGSGTGSGSGTNTENGSNNGSGSGTTNSSGGTNQSGSASGNGSSNSSVSTPDGQHSNPSNPTTSDPKESNPSNPTTSDPKESNPSNPTTSDGQHSNPSNPTTSDPKESNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQNQNK
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Molecular Weight
28.7 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
VlpE is a recombinant protein derived from the pathogenesis of various bacteria, particularly focusing on its role in virulence and immune evasion mechanisms. The study of VlpE has gained prominence due to its potential applications in vaccine development, as it can elicit immune responses that may inhibit bacterial infections. Research has shown that VlpE has a significant role in modulating host immune responses, making it an attractive target for therapeutic interventions. Furthermore, understanding the structure-function relationship of VlpE can provide insights into its interactions with the immune system, offering valuable information for the design of protein-based vaccines. These vaccines could enhance an individual’s protective immunity against bacterial pathogens, thereby contributing to public health efforts to combat infectious diseases. Advances in recombinant DNA technology have enabled the production of VlpE in a controlled laboratory setting, facilitating further experimental studies aimed at elucidating its biological functions and potential as a candidate for vaccine formulation. This research not only helps in identifying key immunogenic regions within the VlpE protein but also lays the groundwork for future developments in molecular medicine and vaccine engineering. As bacterial resistance to conventional antibiotics continues to be a pressing global health challenge, exploring novel vaccine strategies involving VlpE could represent a pivotal shift in the fight against infectious diseases.
