Analytical Data
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基因名
eptA
- Application
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别名
Polymyxin resistance protein PmrC
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种属
Escherichia coli
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P30845
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表达区间
1-547aa
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分子量
64.5 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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 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.












