Analytical Data
-
Gene name
FimF41a
- Application
-
Alternative Names
FimF41a;F41 fimbrial Protein
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P11900
-
Expression Region
23-277aa
-
AA Sequence
ADWTEGQPGDIIIGGEITSPSVKWLWKTGEGLSSFSNTTNEIVKRKLNISVPTDELFLAAKMSDGIKGVFVGNTLIPKIEMASYDGSVITPSFTSNTAMDIAVKVKNSGDNTELGTLSVPLSFGAAVATIFDGDTTDSAVAHIIGGSAGTVFEGLVNPGRFTDQNIAYKWNGLSKAEMAGYVEKLMPGQSASTSYSGFHNWDDLSHSNYTSANKASYLSYGSGVSAGSTLVMNLNKDVAGRLEWVAPVTITVIYS
-
Molecular Weight
34.4 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
FimF41a is a recombinant protein that has garnered significant attention in the field of microbiology and molecular biology due to its potential applications in understanding bacterial adhesion mechanisms. The discovery of FimF41a, a fimbrial adhesin derived from certain pathogenic strains of Escherichia coli, stems from the growing need to combat bacterial infections that frequently arise from biofilm formation on host tissues and medical devices. Fimbriae play a crucial role in the initial adhesion of bacteria to surfaces, facilitating colonization and subsequent infection. Research into FimF41a focuses on its structure, function, and interactions with host cells, which can elucidate the molecular basis of bacterial adherence. By recombinantly expressing this protein, scientists aim to study its biophysical properties and pathogenic potential in vitro, providing insights that could lead to the development of novel therapeutic strategies or vaccines targeting bacterial infections. Moreover, understanding the immunogenicity of FimF41a may also contribute to the design of diagnostic tools or anti-adhesive treatments that can prevent bacterial colonization. Overall, the research on FimF41a not only enhances our fundamental knowledge of bacterial physiology but also holds promise for significant clinical applications in controlling and preventing infectious diseases associated with biofilm-forming bacteria.











