Analytical Data
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Gene name
eptA
- Application
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Alternative Names
Polymyxin resistance protein PmrC
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Species
Escherichia coli
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Source
E. coli
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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
P30845
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Expression Region
1-547aa
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Molecular Weight
64.5 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
The eptA gene encodes a phosphoethanolamine transferase, an enzyme that plays a crucial role in the modification of lipid A, a component of the outer membrane of Gram-negative bacteria. This modification, which involves the addition of phosphoethanolamine groups to lipid A, is a significant mechanism by which bacteria develop resistance to polymyxins, a class of last-resort antibiotics used to treat severe infections. As antibiotic resistance becomes an increasing global health concern, understanding the function and structure of eptA and its encoded protein becomes essential for elucidating the pathways that confer resistance. Research on eptA recombinant protein includes elucidating its enzymatic activity, substrate specificity, and the molecular mechanisms by which it alters lipid A. This involves techniques such as site-directed mutagenesis, protein purification, and structural analysis through methods like X-ray crystallography or cryo-electron microscopy. Such studies provide insights into potential therapeutic targets for overcoming antibiotic resistance, as inhibiting the action of eptA could restore the efficacy of polymyxins against resistant strains. Moreover, the production of eptA recombinant protein not only facilitates the study of its biological function but also aids in the development of rapid diagnostic tools and novel antimicrobial agents that can circumvent existing resistance mechanisms in pathogenic bacteria. Overall, eptA and its recombinant protein represent a critical area of investigation in microbiology and pharmacology, underscoring the urgency of addressing antibiotic resistance in a changing clinical landscape.
