Analytical Data
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Gene name
vacA
- Application
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Alternative Names
vacA; HP_0887; Vacuolating cytotoxin autotransporter [Cleaved into: Vacuolating cytotoxin; Vacuolating cytotoxin translocator]
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Species
Helicobacter pylori
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Source
E. coli
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Tag
N- His-B2M
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P55981
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Expression Region
1018-1290aa
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Molecular Weight
43.6 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
The research on vacA recombinant protein primarily focuses on its role in understanding and combating Helicobacter pylori, a significant pathogen associated with gastric diseases, including peptic ulcers and gastric cancer. The vacA gene encodes a vacuolating cytotoxin, which is crucial for the bacterium's virulence, facilitating its ability to evade the host immune response and contribute to tissue damage. By studying the recombinant forms of the vacA protein, researchers aim to elucidate the mechanisms through which H. pylori exerts its pathogenic effects and to identify specific immune responses generated by the host. This research holds promise for developing novel diagnostic tools and therapeutic strategies to manage H. pylori infections. Furthermore, the generation of vacA recombinant proteins allows for the exploration of their potential use in vaccine development, enabling the induction of protective immunity in individuals at risk of infection. As global prevalence rates of H. pylori remain high, understanding the molecular and immunological aspects of vacA is essential for addressing the public health challenges posed by related gastrointestinal diseases.
