Analytical Data
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Gene name
Type-1A pilin/fimA
- Application
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Alternative Names
Fimbrillin (Fimbrilin) (Major fimbrial subunit protein type I)
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Species
Porphyromonas gingivalis
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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
B2RH54
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Expression Region
47-383aa
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Molecular Weight
43.9 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
Type-1A pili, primarily found in uropathogenic Escherichia coli, are important virulence factors that facilitate bacterial adhesion to host tissues, significantly contributing to urinary tract infections (UTIs). The structural protein that forms these pili, known as Fimbrial Adhesin (FimA), is pivotal in the assembly and function of type-1 pili. Research into Type-1A pilin/FimA recombinant proteins has gained importance due to their potential applications in vaccine development and therapeutic strategies against UTI. This area of study involves elucidating the protein's structure, function, and interaction with host cells, which can provide insights into the mechanisms of bacterial pathogenesis. Moreover, recombinant FimA production using techniques such as recombinant DNA technology allows for the generation of large amounts of the protein, facilitating studies on its immunogenic properties. Understanding the antigenic characteristics of FimA can lead to the design of effective vaccines that elicit strong immune responses, potentially reducing the incidence of UTIs. Additionally, targeted therapies that inhibit the interaction between Type-1A pili and host cellular receptors can be developed, providing alternative strategies to combat bacterial infections. Overall, the study of Type-1A pilin/FimA recombinant proteins promises significant contributions to the fields of microbiology and clinical medicine, addressing urgent public health challenges associated with antibiotic resistance and the prevalence of UTI-causing pathogens.
