Analytical Data
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Gene name
fimA
- Application
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Alternative Names
fimA；Major fimbrium subunit FimA type-1
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04128
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Expression Region
24-182aa
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AA Sequence
AATTVNGGTVHFKGEVVNAACAVDAGSVDQTVQLGQVRTASLAQEGATSS AVGFNIQLNDCDTNVASKAAVAFLGTAIDAGHTNVLALQSSAAGSATNVG VQILDRTGAALTLDGATFSSETTLNNGTNTIPFQARYFATGAATPGAANA DATFKVQYQ
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Molecular Weight
32 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
FimA is a key protein associated with the type 1 fimbriae of uropathogenic Escherichia coli (UPEC), a major cause of urinary tract infections (UTIs). As a virulence factor, FimA plays a critical role in the adhesion of bacteria to the uroepithelium, facilitating colonization and subsequent infection. Research into FimA recombinant protein production has gained momentum due to its potential applications in vaccine development and diagnostic tools. By expressing and purifying FimA in heterologous systems, scientists aim to better understand its structure, function, and interactions with host cells, which is crucial for deciphering the pathogenesis of UPEC. Furthermore, recombinant FimA can be used to elicit immune responses in animal models, providing a pathway for developing effective immunotherapeutics against UTIs. This study aligns with broader efforts to tackle antibiotic resistance by exploring alternative strategies that focus on preventing bacterial adhesion rather than solely relying on traditional antimicrobial treatments. Overall, the investigation of FimA as a recombinant protein not only sheds light on bacterial virulence but also opens avenues for innovative approaches to combat UTIs, ultimately contributing to improved public health outcomes.
