Analytical Data
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Gene name
ybiS
- Application
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Alternative Names
Probable L,D-transpeptidase YbiS(EC 2.-.-.-)
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Species
Escherichia coli O6:H1
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0AAX9
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Expression Region
25-306aa
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Molecular Weight
38.3 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
Related Products
Protein Description
YbiS, a protein characterized in Escherichia coli, is part of a broader study on bacterial stress responses and metabolic regulation. Its significance arises from its potential role in the adaptive mechanisms of bacteria in varying environments. Research has indicated that YbiS may be involved in the response to oxidative stress, influencing the bacterium's ability to survive under detrimental conditions. Understanding YbiS is crucial not only for comprehending bacterial physiology but also for potential biotechnological applications, such as developing bacterial strains with enhanced stress tolerance. Investigating the structure, function, and regulation of YbiS can provide insights into its interactions within the cellular network and its contribution to overall bacterial homeostasis. As antibiotic resistance becomes a pressing global issue, exploring the functions of proteins like YbiS offers novel avenues for intervention strategies, aiming to inhibit bacterial growth or enhance the efficacy of existing treatments. This research underscores the importance of fundamental protein studies in addressing real-world challenges in microbiology and healthcare.
