Analytical Data
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Gene name
fimG
- Application
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Species
Escherichia coli
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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
P08190
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Expression Region
24-167aa
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Molecular Weight
22.3 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
FimG is a vital protein associated with the type 1 fimbriae of uropathogenic Escherichia coli (UPEC), which plays a crucial role in bacterial adhesion to the urinary tract, contributing to urinary tract infections (UTIs). This protein is encoded by the fimbrial operon and is essential for the assembly and stability of fimbrial structures. Research into FimG is significant due to the rising incidence of antibiotic-resistant infections, highlighting the need for alternative therapeutic targets. Understanding the molecular mechanisms underlying FimG's function can aid in the development of new strategies to inhibit bacterial adhesion, thereby preventing UTI recurrence. Furthermore, structural studies of FimG may provide insights into its interactions with other fimbrial components and host tissues. Given the public health implications of UTIs and the challenges posed by multidrug-resistant bacteria, the investigation of FimG and its role in UPEC pathogenesis represents a promising area of research that could lead to innovative treatment approaches and enhance our understanding of bacterial virulence factors.
