Analytical Data
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Gene name
eptA
- Application
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Alternative Names
eptA；pmrC；yjdB；Phosphoethanolamine transferase EptA
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Species
E.coli
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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
P30845
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Expression Region
1-547aa
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AA Sequence
MLKRLLKRPSLNLLAWLLLAAFYISICLNIAFFKQVLQALPLDSLHNVLVFLSMPVVAFSVINIVLTLSSFLWLNRPLACLFILVGAAAQYFIMTYGIVIDRSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWIKIKPATSRLRSVLFRGANILVSVLLILLVAALFYKDYASLFRNNKELVKSLSPSNSIVASWSWYSHQRLANLPLVRIGEDAHRNPLMQNEKRKNLTILIVGETSRAENFSLNGYPRETNPRLAKDNVVYFPNTASCGTATAVSVPCMFSDMPREHYKEELAQHQEGVLDIIQRAGINVLWNDNDGGCKGACDRVPHQNVTALNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQVPMLLWLSEDYQKRYQVDQNCLQKQAQTQHYSQDNLFSTLLGLTGVETKYYQAADDILQTCRRVSE
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Molecular Weight
61.6 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
Related Products
Protein Description
The eptA gene, encoding an enzyme involved in the modification of lipid A in bacterial lipopolysaccharides, has garnered significant attention in recent years due to its role in antibiotic resistance. Specifically, eptA is responsible for the addition of phosphoethanolamine to lipid A, which enhances the survival of bacteria in the presence of cationic antimicrobial peptides. This enzymatic activity can confer resistance to a broad range of antibiotics, making it a critical target for research aimed at combating multidrug-resistant pathogens. The study of eptA and its recombinant protein has implications for understanding bacterial virulence mechanisms and developing novel therapeutic strategies. Researchers are particularly interested in the structural and functional characteristics of the eptA protein, which can provide insights into its enzymatic mechanism and potential inhibitors. By employing advanced techniques such as site-directed mutagenesis, protein purification, and enzymatic assays, scientists aim to elucidate the eptA protein's role in bacterial physiology and its potential as a target for drug development. The growing prevalence of antibiotic-resistant infections underscores the urgency of this research, as it may contribute to the design of effective treatments that circumvent current resistance mechanisms. Ultimately, the exploration of eptA and its recombinant protein holds promise for advancing our understanding of bacterial adaptation and finding new avenues for therapeutic intervention in infectious diseases.
