Analytical Data
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Gene name
vlpE
- Application
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Alternative Names
(VlpE prolipoprotein)
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Species
Mycoplasma hyorhinis
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Source
E. coli
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Tag
N- His & C- Myc
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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
30-109aa
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Molecular Weight
13.9 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, a protein derived from the bacterium *Vibrio parahaemolyticus*, has garnered significant attention in recent years due to its potential roles in pathogenesis and immune response modulation. *Vibrio parahaemolyticus* is known to cause gastrointestinal infections in humans, particularly through the consumption of contaminated seafood. Understanding the structure and function of VlpE is pivotal for elucidating the mechanisms of bacterial virulence and for the development of therapeutic interventions. Research on VlpE has revealed its involvement in cellular processes such as adhesion and biofilm formation, which are crucial for the survival and persistence of the bacteria in host environments. The recombinant expression of VlpE in various systems allows for detailed biochemical and biophysical characterizations, enabling scientists to explore its interaction with host immune components. Additionally, studies have suggested that VlpE may possess immunogenic properties, which could be leveraged in vaccine development. Overall, the investigation of VlpE not only contributes to a deeper understanding of *Vibrio parahaemolyticus* pathophysiology but also holds promise for enhancing public health strategies against foodborne illnesses.
