Analytical Data
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Gene name
Staphopain B
- Application
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Alternative Names
sspB; Z4586; ECs4101Stringent starvation protein B
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Species
Escherichia coli O157:H7
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0AFZ4
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Expression Region
1-165aa
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Molecular Weight
22.3 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
Staphopain B is a cysteine protease secreted by Staphylococcus aureus, a pathogenic bacterium responsible for severe infections in humans. This enzyme plays a crucial role in the pathogenicity of S. aureus, contributing to tissue damage and immune evasion during infection. Given its significance, Staphopain B has gained attention as a potential therapeutic target and diagnostic marker. Researchers have focused on the recombinant expression of Staphopain B to study its enzymatic properties, substrate specificity, and interactions with host proteins. The recombinant protein offers insights into the enzyme's structure-function relationship and facilitates the development of specific inhibitors, which could lead to novel treatments against staphylococcal infections. Additionally, understanding the molecular mechanisms of Staphopain B could aid in designing vaccines or immunotherapies, thereby enhancing our ability to combat S. aureus-related diseases. Overall, the investigation of Staphopain B's biochemical characteristics and its role in pathogenesis is critical for advancing our knowledge of bacterial proteases and developing strategies to mitigate bacterial infections.
