Analytical Data
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Gene name
yihF
- Application
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Alternative Names
yihF; b3861; JW5574; Uncharacterized protein YihF
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P32128
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Expression Region
25-476aa
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Molecular Weight
66.1 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
YihF is a well-characterized protein in Escherichia coli that has garnered significant interest due to its role in regulating bacterial motility and biofilm formation. Research has shown that YihF functions as a regulatory protein in the bacterial signaling pathways, particularly in response to environmental stresses. It is believed to inhibit flagellar gene expression, thus influencing the switch between motile and sessile lifestyles in E. coli. Insights into its structure and function are critical for understanding bacterial adaptive mechanisms and could potentially inform the development of novel antimicrobial strategies. Recombination techniques to express YihF as a recombinant protein provide a valuable tool for studying its biochemical properties and interactions with other cellular components. Characterizing YihF's structure through methods such as X-ray crystallography or NMR spectroscopy can reveal important details about its functional domains and regulatory mechanisms. Furthermore, studying YihF in various conditions helps elucidate its role in pathogenesis and bacterial communication, making it a target of interest in the field of microbiology and biotechnology. Understanding YihF's activities and regulatory networks could illuminate broader aspects of microbial ecology and the evolution of bacterial behavior. Overall, the recombinant expression and study of YihF could contribute significantly to our understanding of bacterial biology and lead to practical applications in combating bacterial infections.
