Analytical Data
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Gene name
PEO1
- Application
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Alternative Names
Progressive external ophthalmoplegia 1 protein;T7 gp4-like protein with intramitochondrial nucleoid localization;T7-like mitochondrial DNA helicase
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96RR1
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Expression Region
32-684aa
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Molecular Weight
75.5 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
PEO1 is a recombinant protein derived from the Pseudomonas aeruginosa, a common bacterium known for its role in various infections and its capacity to degrade environmental pollutants. The study of PEO1 has gained traction due to its potential applications in biotechnology and medicine, particularly in understanding bacterial resistance mechanisms and developing novel therapeutic strategies. This protein is involved in critical biochemical pathways that contribute to the survival of Pseudomonas in harsh environments, making it a focal point for research aimed at combating antibiotic resistance. Additionally, PEO1 may serve as a model for exploring the interactions between pathogens and host systems, enhancing our understanding of infectious diseases. The expression and purification of PEO1 as a recombinant protein facilitate detailed structural and functional analyses, allowing researchers to investigate its properties, interactions, and potential as a drug target or diagnostic tool. Ongoing studies aim to elucidate the mechanisms by which PEO1 exerts its effects, thereby contributing to the development of innovative approaches to tackle bacterial infections and enhance bioremediation efforts. As antibiotic resistance continues to pose a significant challenge to public health, the exploration of proteins like PEO1 is essential for advancing our biomedical knowledge and developing effective interventions.
