Analytical Data
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Gene name
pvdA
- Application
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Alternative Names
L-ornithine N(5)-hydroxylase L-ornithine N(5)-oxygenase Pyoverdin biosynthesis protein A
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Species
Pseudomonas aeruginosa
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q51548
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Expression Region
1-443aa
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Molecular Weight
65.5 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
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Protein Description
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.
