关键信息
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基因名
pvdA
- 应用
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别名
L-ornithine N(5)-hydroxylase L-ornithine N(5)-oxygenase Pyoverdin biosynthesis protein A
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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
Q51548
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表达区间
1-443aa
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分子量
65.5 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.
质检流程
相关产品
背景信息
The PvdA protein, a key component of the pyoverdine biosynthetic pathway in Pseudomonas aeruginosa, has garnered significant attention in recent research due to its critical role in iron acquisition and virulence. Pseudomonas aeruginosa, an opportunistic pathogen, thrives in various environments, particularly in immunocompromised hosts, by utilizing pyoverdine—a high-affinity iron-chelating molecule. The PvdA enzyme is responsible for the enzymatic transformation of precursor molecules into pyoverdine, which not only facilitates iron uptake but also influences the bacterium’s ability to establish infections. Given the increasing prevalence of antibiotic-resistant strains of P. aeruginosa, understanding the mechanisms of pyoverdine synthesis and the function of PvdA can aid in developing novel therapeutic strategies. Furthermore, insights into PvdA structure and function could potentially reveal new targets for drug development, highlighting its importance in microbial pathogenesis and antibiotic resistance. Recent advancements in molecular biology and protein engineering have enabled researchers to study PvdA more comprehensively, paving the way for innovative approaches in combating infections caused by this resilient pathogen. Overall, the investigation of PvdA and its associated pathways not only enhances our understanding of bacterial iron metabolism but also presents promising avenues for therapeutic intervention against P. aeruginosa infections.
