Analytical Data
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Gene name
fimH
- Application
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Alternative Names
fimH；Pancreatic secretory granule membrane major glycoProtein GP2
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Species
Human
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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
P37925
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Expression Region
23-335aa
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AA Sequence
TVCRNSNGTATDIFYDLSDVFTSGNNQPGQVVTLPEKSGWVGVNATCPAGTTVNYTYRSYVSELPVQSTEGNFKYLKLNDYLLGAMSITDSVAGVFYPPRNYILMGVDYNVSQQKPFGVQDSKLVFKLKVIRPFINMVTIPRQTMFTVYVTTSTGDALSTPVYTISYSGKVEVPQNCEVNAGQVVEFDFGDIGASLFSQAGAGNRPQGVTPQTKTIAIKCTNVAAQAYLSMRLEAEKASGQAMVSDNPDLGFVVANSNGTPLTPNNLSSKIPFHLDDNAAARVGIRAWPISVTGIKPAEGPFTARGYLRVDYD
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Molecular Weight
41.2 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
FimH is an adhesin found on the type 1 fimbriae of uropathogenic Escherichia coli (UPEC), a major cause of urinary tract infections (UTIs). This protein plays a crucial role in the initial adherence of bacteria to the host's uroepithelial cells, facilitating colonization and subsequent infection. Research into FimH has gained significant attention due to its implications in understanding the mechanisms of bacterial pathogenesis and the development of targeted therapeutic strategies. FimH has been identified as a potential vaccine candidate, as inhibiting its function could prevent UPEC from attaching to urinary tract tissues. The characterization of FimH and the study of its interactions with host receptors have advanced significantly with the advent of recombinant protein technology. By producing and purifying recombinant FimH, researchers can investigate its structure, stability, and function in detail while exploring potential inhibitors that could disrupt its binding capabilities. This research not only enhances our understanding of UPEC infections but also paves the way for innovative approaches to combat UTIs, which are prevalent and can lead to serious complications, especially in vulnerable populations. Overall, the study of FimH as a recombinant protein serves as a bridge between basic microbiology and clinical applications, providing insights that could lead to improved prevention and treatment of urinary tract infections.
