Analytical Data
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Gene name
ompD
- Application
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Alternative Names
ompD；Uridine 5'-monophosphate synthase
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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
P37592
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Expression Region
22-362aa
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AA Sequence
AEVYNKDGNKLDLYGKVHAQHYFSDDNGSDGDKTYARLGFKGETQINDQLTGFGQWEYEFKGNRTESQGADKDKTRLAFAGLKFADYGSFDYGRNYGVAYDIGAWTDVLPEFGGDTWTQTDVFMTGRTTGVATYRNTDFFGLVEGLNFAAQYQGKNDRDGAYESNGDGFGLSATYEYEGFGVGAAYAKSDRTNNQVKAASNLNAAGKNAEVWAAGLKYDANNIYLATTYSETLNMTTFGEDAAGDAFIANKTQNFEAVAQYQFDFGLRPSIAYLKSKGKNLGTYGDQDLVEYIDVGATYYFNKNMSTFVDYKINLLDDSDFTKAAKVSTDNIVAVGLNYQF
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Molecular Weight
53.6 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
OmpD is a porin protein found in the outer membrane of certain Gram-negative bacteria, primarily Escherichia coli, and plays a crucial role in the transport of small molecules and ions. The significance of OmpD in bacterial physiology and pathogenesis has attracted considerable research interest, especially in understanding antibiotic resistance mechanisms and developing novel antibacterial strategies. As antibiotic resistance becomes an increasingly critical global health issue, the characterization of outer membrane proteins like OmpD is essential not only for elucidating bacterial nutrient uptake and environmental adaptation but also for identifying potential targets for drug development. The recombinant expression of OmpD in heterologous systems, such as E. coli or yeast, allows for detailed studies of its structure, function, and interaction with other molecules. Additionally, studies involving OmpD can provide insights into the evolutionary adaptations of bacteria in response to changing environments and selective pressures. The exploration of OmpD may also inform vaccine development strategies, as outer membrane proteins can serve as immunogenic targets. Therefore, investigating OmpD in depth has the potential to contribute to both fundamental microbiology and applied biomedical research, making it a relevant subject in contemporary studies related to infectious diseases and antibiotic resistance strategies.
