Analytical Data
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Gene name
Stfa2
- Application
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Alternative Names
Stfa2; Stf-2; Stf2Stefin-2
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Species
Mouse
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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
P35174
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Expression Region
1-103aa
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Molecular Weight
17.1 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
Stfa2 is a recombinant protein derived from the Staphylococcus aureus bacterium, and its research has garnered significant attention due to its potential applications in microbiology and biotechnology. As a key component of the bacterium's immune evasion mechanisms, Stfa2 functions as a virulence factor that may inhibit the host's immune response, making it a target for therapeutic intervention. Understanding the structure and function of Stfa2 is crucial for developing novel strategies to combat Staphylococcus aureus infections, which are known for their clinical significance and rising antibiotic resistance. Additionally, recombinant technology allows for the production of Stfa2 in controlled laboratory settings, facilitating detailed studies of its biochemical properties and interactions with immune cells. This research is essential not only for developing effective vaccines and therapies against Staphylococcus aureus but also for enhancing our understanding of pathogenic mechanisms employed by bacterial pathogens. Insights gained from Stfa2 studies could contribute to broader applications in vaccine development and immune modulation, thus addressing public health challenges associated with bacterial infections. Overall, the investigation of Stfa2 as a recombinant protein represents a promising frontier in infectious disease research, with implications for both clinical treatment and basic science.











