Analytical Data
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Gene name
pilA
- Application
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Alternative Names
(Pilin)
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Species
Pseudomonas aeruginosa
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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
P04739
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Expression Region
28-149aa
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Molecular Weight
20.1 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
The study of PilA recombinant protein has gained significant attention due to its essential role in the formation of pili, which are hair-like structures that extend from the surface of bacteria. These pili play a crucial role in various bacterial functions, including adherence to host tissues, biofilm formation, and genetic exchange, which are critical for bacterial virulence and pathogenicity. Understanding the structure and function of PilA is particularly important in the context of bacterial infections, as targeting pili-mediated interactions could lead to novel therapeutic strategies. Furthermore, PilA has implications in biotechnology, where its ability to facilitate surface attachment makes it a valuable tool for developing biosensors and biocatalysts. Recent advances in genetic engineering and protein purification techniques have enabled the production of high-quality PilA recombinant proteins, allowing for detailed studies of their biochemical properties and interactions. Research into PilA also focuses on its immunogenic potential, providing insights into vaccine development against pili-expressing pathogens. Overall, the multifaceted role of PilA in microbial behavior and its applications in medicine and biotechnology make it a critical subject of study in molecular microbiology and related fields.
