Analytical Data
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Gene name
yebF
- Application
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Alternative Names
yebF；Protein YebF
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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
P33219
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Expression Region
22-118aa
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AA Sequence
ANNETSKSVTFPKCEDLDAAGIAASVKRDYQQNRVARWADDQKIVGQADP VAWVSLQDIQGKDDKWSVPLTVRGKSADIHYQVSVDCKAGMAEYQRR
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Molecular Weight
16 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
Related Products
Protein Description
The study of the yebF recombinant protein has gained significance in the context of understanding bacterial virulence and stress response mechanisms. yebF, a gene found in various bacterial species, is implicated in processes such as biofilm formation and resistance to oxidative stress. Researchers have identified yebF as a potential player in the regulation of gene expression and cellular responses to environmental challenges, making it a target for further investigation. The protein's structure and function, as well as its interactions with other cellular components, remain relatively unexplored, presenting a valuable opportunity for research. By characterizing the yebF recombinant protein, scientists aim to elucidate its role in bacterial physiology, which could pave the way for novel therapeutic strategies against pathogenic bacteria. Understanding the molecular underpinnings of yebF could also contribute to the broader field of microbiology by providing insights into bacterial adaptation mechanisms, ultimately leading to improved control measures in both clinical and industrial settings.
