Analytical Data
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Gene name
vpl1
- Application
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Alternative Names
(Versatile liquid phase peroxidase 1)
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Species
Pleurotus eryngii
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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
Q9UR19
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Expression Region
31-361aa
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Molecular Weight
42.0 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
Vpl1, an important protein derived from various viral and bacterial origins, has garnered significant attention in the field of molecular biology due to its potential applications in therapeutics and biotechnology. Research surrounding Vpl1 focuses on its role in pathogen interaction, immune response modulation, and its utility as a recombinant protein for vaccine development. The interest in Vpl1 stems from its unique structural features and functional properties, which allow for a deeper understanding of protein interactions and cellular mechanisms. Furthermore, advances in recombinant DNA technology have enabled the production of Vpl1 in various expression systems, facilitating in-depth studies of its biochemical characteristics and biological activities. This recombinant approach not only enhances the yield of Vpl1, allowing for large-scale applications but also enables the exploration of its modified versions with enhanced efficacy. As researchers continue to investigate Vpl1, its potential applications are expanding to include use in diagnostic tools, therapeutic agents, and as a model for studying viral and bacterial pathogenesis. Thus, the study of Vpl1 recombinant protein is not only critical for developing effective therapeutic strategies but also serves as a significant avenue for understanding the complexities of host-pathogen interactions in diverse biological systems.
