Analytical Data
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基因名
oprP
- Application
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别名
Outer membrane protein D1
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种属
Pseudomonas aeruginosa
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P05695
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表达区间
30-440aa
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分子量
61.2 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
OprP is a porin protein found in the outer membrane of Pseudomonas aeruginosa, an opportunistic pathogen known for its resistance to multiple antibiotics. This protein plays a critical role in the transport of small molecules, such as phosphate and some antibiotics, across the bacterial membrane, thereby influencing the bacterium's growth, virulence, and drug susceptibility. The study of OprP and its recombinant forms has gained significance due to the increasing prevalence of multidrug-resistant strains of P. aeruginosa, which pose a significant threat in clinical settings, particularly for immunocompromised patients. Understanding the structure and function of OprP can provide insights into its mechanisms of action and interaction with various substrates, which may lead to the identification of novel therapeutic targets. Research has focused on the characterization of OprP’s molecular structure, its transport dynamics, and its role in biofilm formation—a key factor in the pathogenesis of P. aeruginosa infections. Moreover, recombinant OprP can serve as a valuable tool for studying porin function and for developing new strategies to combat bacterial infections. The ongoing investigation into OprP aims to elucidate its potential as a target for drug design and to enhance our overall understanding of bacterial membrane transport processes.












