Analytical Data
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Gene name
hlgA
- Application
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Alternative Names
H-gamma-2 (H-gamma-II) (hlg2)
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Species
Staphylococcus aureus
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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
P0A073
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Expression Region
30-309aa
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Molecular Weight
39.4 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
The study of HlgA recombinant protein is rooted in the quest to understand the mechanisms of bacterial virulence and the potential development of novel therapeutic strategies. HlgA, a member of the alpha-hemolysin family produced by Staphylococcus aureus, is a significant factor contributing to the pathogenicity of this bacterium, which is notorious for causing a wide range of infections in humans, from mild skin infections to severe conditions like pneumonia and sepsis. Given the rising prevalence of antibiotic-resistant strains of S. aureus, particularly methicillin-resistant Staphylococcus aureus (MRSA), there is an urgent need for alternative treatment measures. Research on HlgA aims to elucidate its structure-function relationships, cellular interactions, and the immune responses it elicits. By producing recombinant HlgA for detailed biochemical and biophysical studies, researchers can explore its role in cell lysis and tissue damage, as well as evaluate its potential as a target for vaccine development or therapeutic intervention. Furthermore, understanding how HlgA interacts with host immune cells can shed light on the strategies employed by S. aureus to evade immune detection, which is crucial for formulating effective preventive measures. Overall, the investigation of HlgA not only enhances our fundamental knowledge of bacterial pathogenesis but also holds promising implications for addressing the growing challenge of antibiotic resistance in clinical settings.
