Analytical Data
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Gene name
oppA
- Application
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Alternative Names
oppA；Periplasmic oligopeptide-binding Protein OppA
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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
P23843
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Expression Region
27-543aa
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AA Sequence
ADVPAGVTLAEKQTLVRNNGSEVQSLDPHKIEGVPESNISRDLFEGLLVSDLDGHPAPGVAESWDNKDAKVWTFHLRKDAKWSDGTPVTAQDFVYSWQRSVDPNTASPYASYLQYGHIAGIDEILEGKKPITDLGVKAIDDHTLEVTLSEPVPYFYKLLVHPSTSPVPKAAIEKFGEKWTQPGNIVTNGAYTLKDWVVNERIVLERSPTYWNNAKTVINQVTYLPIASEVTDVNRYRSGEIDMTNNSMPIELFQKLKKEIPDEVHVDPYLCTYYYEINNQKPPFNDVRVRTALKLGMDRDIIVNKVKAQGNMPAYGYTPPYTDGAKLTQPEWFGWSQEKRNEEAKKLLAEAGYTADKPLTINLLYNTSDLHKKLAIAASSLWKKNIGVNVKLVNQEWKTFLDTRHQGTFDVARAGWCADYNEPTSFLNTMLSNSSMNTAHYKSPAFDSIMAETLKVTDEAQRTALYTKAEQQLDKDSAIVPVYYYVNARLVKPWVGGYTGKDPLDNTYTRNMYIVKH
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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 the oppA protein, part of the oligopeptide permease (Opp) system, has garnered significant interest due to its role in bacterial peptide transport and its potential implications in antimicrobial resistance and pathogenesis. OppA is a periplasmic binding protein that plays a crucial role in the uptake of heterogeneous peptides, which are vital for bacterial growth, survival, and virulence. Understanding the mechanisms underlying the peptide transport system can provide insights into how bacteria adapt and proliferate in various environments, including host organisms. Given the rise of antibiotic-resistant strains, exploring oppA and its functional properties offers a pathway to identify novel targets for therapeutic intervention. Furthermore, recombinant expression of oppA protein allows for in-depth structural and functional analyses, facilitating the identification of its binding affinities and conformational dynamics. Studies utilizing recombinant oppA protein not only enhance our comprehension of peptide transport mechanisms but also contribute to the development of innovative strategies to combat bacterial infections, as well as improve our understanding of the evolutionary mechanisms that underpin bacterial adaptability. Overall, the research on oppA recombinant protein is pivotal for both basic science in microbiology and applied biomedical fields, particularly in the context of developing new antimicrobial strategies.
