Analytical Data
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Gene name
oppA
- Application
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Alternative Names
/
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23843
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Expression Region
27-543aa
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Molecular Weight
65.8 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 reconstituted OppA (oligopeptide transporter A) proteins has garnered significant attention in the fields of microbiology and biochemistry due to their critical role in the transport and utilization of peptides in various bacterial species. OppA acts as a periplasmic binding protein that specifically binds to oligopeptides and is an essential component of the oligopeptide transport system, which is pivotal for nutrient acquisition and signal transduction in bacteria. Understanding OppA's structure and function can provide insights into the mechanisms of peptide uptake, which is vital for bacterial growth, survival, and pathogenicity. Moreover, OppA has potential applications in biotechnology and medicine, such as in the development of targeted antibiotic therapies and protein engineering. Recent advancements in techniques like X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy have allowed researchers to elucidate the three-dimensional structures of OppA, revealing its binding sites and conformational changes upon peptide interaction. These studies not only enhance our knowledge of transport mechanisms but may also facilitate the design of inhibitors that can disrupt peptide transport in pathogenic bacteria, paving the way for innovative antimicrobial strategies. Therefore, investigating the reconstitution and functionality of OppA proteins is crucial for both fundamental research and the development of practical applications in combating bacterial infections.
