Analytical Data
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Gene name
oxyR
- Application
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Alternative Names
oxyR; Probable hydrogen peroxide-inducible genes activator
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Species
Streptomyces viridosporus
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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
Q9X5P2
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Expression Region
1-312aa
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Molecular Weight
40.6 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
OxyR is a transcriptional regulator that plays a crucial role in the oxidative stress response in various bacteria, particularly in Escherichia coli and other related species. This protein acts as a redox sensor, enabling bacteria to adapt to oxidative stress conditions by regulating the expression of genes involved in detoxifying reactive oxygen species (ROS). Research on OxyR has gained attention due to its importance in bacterial survival under stress conditions, its potential role in pathogenesis, and its implications in antibiotic resistance. The understanding of OxyR's structure and function is vital for elucidating the mechanisms by which bacteria protect themselves from oxidative damage. Recombinant OxyR protein studies contribute significantly to this field by allowing researchers to investigate its biochemical properties, regulatory mechanisms, and interactions with other molecular players in the oxidative stress response. By expressing OxyR as a recombinant protein, scientists can employ techniques such as X-ray crystallography, NMR spectroscopy, and mutagenesis studies to unravel the details of its functionality, which can further enhance our understanding of bacterial physiology and resistance mechanisms. Additionally, insights gained from OxyR research may lead to the development of novel antimicrobial strategies aimed at targeting the oxidative stress response pathways in pathogenic bacteria. As bacterial resistance to conventional antibiotics continues to rise, targeting the regulatory systems like that of OxyR presents a promising avenue for new therapeutic interventions, making this research not only relevant to fundamental microbiology but also to public health concerns worldwide.
