Analytical Data
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Gene name
vlpF
- Application
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Alternative Names
(VlpF prolipoprotein)
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Species
Mycoplasma hyorhinis
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Source
E. coli
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Tag
N- His-KSI
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q49538
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Expression Region
30-67aa
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Molecular Weight
18.9 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
VlpF is a protein of interest derived from the Vibrio cholerae bacterium, which is known for its role in the pathogenicity of cholera. Research on VlpF has gained attention due to its involvement in the bacterial adhesive mechanisms that facilitate colonization and infection in host organisms. The protein’s structure and function have been characterized to understand its contribution to biofilm formation and virulence. Moreover, VlpF shows potential as a target for novel therapeutic strategies, aiming to disrupt bacterial adhesion and biofilm integrity. The recombinant production of VlpF allows for detailed studies into its biochemical properties, interaction with host cells, and role in immune response. Understanding the molecular dynamics of VlpF is essential for developing vaccines or interventions against cholera, which remains a significant global health issue. Overall, exploring VlpF through recombinant protein technology not only enhances our comprehension of bacterial pathogenesis but also opens doors to innovative solutions for cholera prevention and treatment.
