Analytical Data
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Gene name
hlyE
- Application
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Alternative Names
Cytotoxin ClyA;Hemolysis-inducing protein;Latent pore-forming 34 kDa hemolysin;Silent hemolysin SheA
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Species
Escherichia coli
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Source
E. coli
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P77335
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Expression Region
2-182aa
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Molecular Weight
21.2 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
HlyE, a member of the RTX (Repeats in ToXin) toxin family, is produced by certain pathogenic bacteria, notably within the family of enterobacteria. Research into HlyE has gained significant attention due to its role in bacterial virulence, particularly its ability to form pores in host cell membranes, leading to cell lysis and contributing to tissue damage during infection. Understanding the mechanisms of HlyE, including its structure and interaction with host cells, is crucial for developing strategies to combat infections caused by HlyE-producing pathogens. Recent studies have focused on the recombinant expression of HlyE to produce sufficient quantities for detailed biochemical and structural analysis. This recombinant protein can be used to investigate its functional properties, elucidate its pathogenic mechanisms, and screen for potential inhibitors that might mitigate its harmful effects. Furthermore, the study of HlyE may also contribute to vaccine development or therapeutic interventions against enterobacterial infections. As antibiotic resistance becomes a growing concern in modern medicine, research on HlyE and similar virulence factors is essential for devising new strategies to treat bacterial infections effectively.
