Analytical Data
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Gene name
F17a-A
- Application
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Alternative Names
F17 fimbrial adhesive antigen F17 pilin
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11312
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Expression Region
22-180aa
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Molecular Weight
32.4 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
Related Products
Protein Description
The F17a-A recombinant protein has emerged as a significant focus in the field of molecular biology and immunology due to its potential applications in vaccine development and therapeutic interventions. This protein is derived from the F17a gene region of pathogenic strains of bacteria, particularly in relation to its role in stimulating immune responses. Research has shown that F17a-A possesses unique antigenic properties, making it a promising candidate for eliciting specific antibodies that can neutralize bacterial infections. The ability to produce this protein in a recombinant form allows for large-scale purification and characterization, facilitating detailed studies on its structural and functional characteristics. Moreover, the use of recombinant technology enables the modification of the protein to enhance its immunogenicity, thereby improving vaccine efficacy. Given the rising concern over antibiotic resistance and the need for innovative therapeutic solutions, the F17a-A recombinant protein represents a critical component in the development of novel immunotherapeutic approaches. Ongoing studies aim to elucidate the precise mechanisms by which F17a-A interacts with the immune system, paving the way for its application in clinical settings. This research is vital for advancing our understanding of host-pathogen interactions and can potentially lead to the creation of effective vaccines and treatments against bacterial pathogens that pose significant health threats globally.
