Analytical Data
-
Gene name
fimC
- Application
-
Alternative Names
fimC；Chaperone Protein FimC
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P31697
-
Expression Region
37-241aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMGVALGATRVIYPAGQKQEQLAVTNNDENS TYLIQSWVENADGVKDGRFIVTPPLFAMKGKKENTLRILDATNNQLPQDR ESLFWMNVKAIPSMDKSKLTENTLQLAIISRIKLYYRPAKLALPPDQAAE KLRFRRSANSLTLINPTPYYLTVTELNAGTRVLENALVPPMGESTVKLPS DAGSNITYRTINDYGALTPKMTGVME
-
Molecular Weight
25 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
The study of fimC recombinant protein is situated within the broader context of microbial pathogenesis and host-pathogen interactions. fimC is a key gene involved in the biosynthesis of fimbriae, which are hair-like structures on the surface of certain bacteria, such as Escherichia coli. These fimbriae facilitate adhesion to host tissues and are critical for the establishment of infections, particularly in the urinary tract. Research on fimC recombinant protein is essential for understanding the molecular mechanisms of bacterial adherence and the potential for developing novel therapeutic strategies. By producing fimC as a recombinant protein, scientists can study its structure and function in detail, elucidate its role in biofilm formation, and explore its potential as a vaccine candidate. Understanding the immunogenic properties of the fimC protein may also lead to the design of new diagnostic tools and therapeutic interventions aimed at preventing bacterial infections. Consequently, the investigation of fimC recombinant protein not only contributes to our fundamental knowledge of bacterial biology but also holds promise for addressing significant public health issues related to antibiotic resistance and recurrent infections.
