Analytical Data
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Gene name
yopH
- Application
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Alternative Names
Virulence protein
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Species
Yersinia enterocolitica
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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
P15273
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Expression Region
1-468aa
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Molecular Weight
58.4 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
YopH is a well-characterized virulence factor secreted by the pathogenic bacterium Yersinia pestis, the causative agent of plague, and Yersinia pseudotuberculosis. This protein functions as a tyrosine phosphatase and plays a crucial role in disrupting host cell signaling pathways, enabling the bacteria to evade the host's immune response. The interest in YopH arises from its potential to provide insights into bacterial pathogenesis and immune evasion mechanisms, which could lead to the development of novel therapeutic strategies or vaccines. Moreover, the study of YopH can contribute to a broader understanding of phosphatase functions in cellular processes. Research involves the recombinant expression of YopH in various systems, allowing for functional assays, structural analysis, and the exploration of its inhibitory mechanisms. Furthermore, the investigation into YopH has implications for understanding other diseases caused by similar mechanisms of immune system manipulation, making it a significant target for both basic research and applied biomedical science. The multifaceted role of YopH in host-pathogen interactions underscores its importance as a model for investigating bacterial virulence factors.
