Analytical Data
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Gene name
ytfE
- Application
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Alternative Names
ytfE；Iron-sulfur cluster repair Protein YtfE
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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
P69506
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Expression Region
1-220aa
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AA Sequence
MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE
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Molecular Weight
51.9 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
The study of YtfE, a recombinant protein, has emerged as a focal point in microbial physiology and protein biochemistry due to its pivotal role in the cellular response to oxidative stress. YtfE is primarily characterized as a putative peroxidase that has been linked to the maintenance of cellular redox balance in bacteria. This protein is particularly noteworthy in Escherichia coli, where it participates in the repair of oxidized proteins, thus playing a crucial role in preserving cellular integrity under stress conditions. The ability of YtfE to facilitate the reductive repair of damaged proteins underscores its potential importance in bacterial survival and adaptation. Additionally, the exploration of YtfE has broad implications for understanding the mechanisms of oxidative damage and repair in both prokaryotic and eukaryotic systems. The recombinant expression of YtfE allows for detailed kinetic studies and structural analyses, leading to insights into its enzymatic functions and substrate specificity. Given the increasing prevalence of oxidative stress-related diseases in humans, research on YtfE and similar proteins may contribute to the development of novel therapeutic strategies. Overall, the investigation of YtfE not only enhances our comprehension of microbial resilience mechanisms but also paves the way for applications in biotechnology and medicine, highlighting the importance of this recombinant protein in both fundamental and applied research contexts.
