Analytical Data
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Gene name
yfbU
- Application
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Species
Escherichia coli O6:H1
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Source
E. coli
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Tag
N- MBP & C- His-Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A8W9
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Expression Region
1-164aa
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Molecular Weight
67.3 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
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Protein Description
YfbU protein is a conserved bacterial protein that has garnered interest due to its potential roles in cell membrane integrity and antibiotic resistance. Research has indicated that YfbU is involved in regulating the peptidoglycan layer, a crucial component of bacterial cell walls, which not only provides structural support but also plays a significant role in protecting against external stresses and antibiotics. Studies have shown that mutations in the yfbU gene can lead to altered susceptibility to various antibiotics, suggesting that this protein may be a key player in bacterial adaptation and survival mechanisms. Additionally, the functional characterization of YfbU could unveil new targets for antimicrobial drug development, particularly in an era where antibiotic resistance poses a significant threat to public health. Understanding the structure and function of YfbU at the molecular level may also provide insights into its interactions with other cellular components, helping to elucidate its role in bacterial physiology and pathogenesis. Thus, the ongoing research into YfbU protein not only contributes to our fundamental knowledge of bacterial biology but also holds promise for advancing therapeutic strategies against resistant strains.
