Analytical Data
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Gene name
pvdA
- Application
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Alternative Names
pvdA；pvd-1；L-ornithine N(5)-monooxygenase
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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
Q51548
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Expression Region
1-443aa
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AA Sequence
MTQATATAVVHDLIGVGFGPSNIALAIALQERAQAQGALEVLFLDKQGDYRWHGNTLVSQSELQISFLKDLVSLRNPTSPYSFVNYLHKHDRLVDFINLGTFYPCRMEFNDYLRWVASHFQEQSRYGEEVLRIEPMLSAGQVEALRVISRNADGEELVRTTRALVVSPGGTPRIPQVFRALKGDGRVFHHSQYLEHMAKQPCSSGKPMKIAIIGGGQSAAEAFIDLNDSYPSVQADMILRASALKPADDSPFVNEVFAPKFTDLIYSREHAERERLLREYHNTNYSVVDTDLIERIYGVFYRQKVSGIPRHAFRCMTTVERATATAQGIELALRDAGSGELSVETYDAVILATGYERQLHRQLLEPLAEYLGDHEIGRDYRLQTDERCKVAIYAQGFSQASHGLSDTLLSVLPVRAEEISGSLYQHLKPGTAARALHEHALAS
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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
Related Products
Protein Description
The study of the PvdA recombinant protein is rooted in the increasing interest in the mechanisms of iron acquisition in bacteria, particularly in pathogenic species that rely on siderophores to sequester iron from the host environment. PvdA, an enzyme found in Pseudomonas aeruginosa, plays a critical role in the biosynthesis of the siderophore pyoverdine, which is essential for the bacteria’s virulence and survival in iron-limited conditions. Understanding the structure and function of PvdA not only provides insights into microbial iron homeostasis but also sheds light on potential therapeutic targets for combating infections caused by Pseudomonas aeruginosa, a notable opportunistic pathogen in various healthcare settings. The recombinant production of PvdA allows for detailed biochemical characterization and structural analysis, facilitating the exploration of its enzymatic mechanisms, substrate interactions, and regulatory pathways. This research contributes to the broader field of bacterial pathogenesis and iron metabolism, opening avenues for the development of novel antimicrobial strategies that could mitigate the rising concerns of antibiotic resistance in clinical environments.
