Analytical Data
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Gene name
lptE
- Application
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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
C4ZWC8
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Expression Region
19-193aa
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Molecular Weight
26.9 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 research on recombinant LptE protein stems from its essential role in the endotoxin transport pathway within Gram-negative bacteria. LptE, part of the lipopolysaccharide transport system, specifically contributes to the translocation of lipopolysaccharides (LPS) across the outer membrane, a critical process for bacterial virulence and immune evasion. Understanding LptE's structure and function can provide valuable insights into bacterial membrane biology and the mechanisms of LPS assembly. With the rise of antibiotic resistance among pathogenic Gram-negative bacteria, elucidating the transport mechanisms of LptE also holds potential for developing novel antimicrobial strategies. By employing recombinant DNA technology, researchers can produce LptE in vitro, facilitating detailed biochemical and biophysical analyses. These studies may reveal the protein's interactions with other components of the LPS transport machinery, offering the possibility of targeting LptE in drug design efforts. As such, LptE not only represents a key element in basic microbiological research but also serves as a target for therapeutic intervention in the fight against resistant bacterial infections.
