Analytical Data
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Gene name
VACWR150
- Application
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Alternative Names
VACWR150；Protein OPG154
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Species
E.coli
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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
P11258
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Expression Region
1-110aa
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AA Sequence
MDGTLFPGDDDLAIPATEFFSTKAAKKPEAKREAIVKADEDDNEETLKQRLTNLEKKITNVTTKFEQIEKCCKRNDEVLFRLENHAETLRAAMISLAKKIDVQTGRRPYE
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Molecular Weight
17.6 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
VACWR150 is a recombinant protein derived from the Vibrio alginolyticus toxin, which has garnered significant interest in the field of infectious disease research due to its potential applications in vaccine development and therapeutic interventions. Vibrio alginolyticus is a bacterium known to cause gastrointestinal infections, particularly in immunocompromised individuals. The VACWR150 protein is part of ongoing studies aimed at understanding the immune response elicited by Vibrio infections. Researchers are investigating its structural properties, antigenicity, and the pathways through which it may trigger an immune response. By characterizing this protein, scientists hope to identify novel vaccine candidates that can offer protection against Vibrio-related diseases. Additionally, the recombinant nature of VACWR150 allows for its production in controlled laboratory settings, facilitating large-scale studies and enabling the assessment of its efficacy in preclinical models. As antibiotic resistance becomes a growing concern in treating bacterial infections, VACWR150 represents a promising avenue for developing new strategies to combat Vibrio infections, aiming to reduce morbidity and mortality rates associated with these illnesses. The exploration of VACWR150 not only enhances our understanding of host-pathogen interactions but also contributes to the broader field of immunology and vaccine research, paving the way for innovative therapeutic solutions in the fight against bacterial pathogens.
