Analytical Data
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Gene name
lptA
- Application
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Alternative Names
lptA；yhbN；Lipopolysaccharide export system Protein LptA
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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
P0ADV1
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Expression Region
28-185aa
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AA Sequence
VTGDTDQPIHIESDQQSLDMQGNVVTFTGNVIVTQGTIKINADKVVVTRPGGEQGKEVIDGYGKPATFYQMQDNGKPVEGHASQMHYELAKDFVVLTGNAYLQQVDSNIKGDKITYLVKEQKMQAFSDKGKRVTTVLVPSQLQDKNNKGQTPAQKKGN
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Molecular Weight
19.3 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
LptA is an essential protein involved in the transport of lipopolysaccharides (LPS) to the outer membrane of Gram-negative bacteria, playing a crucial role in maintaining bacterial integrity and virulence. Research on LptA has gained prominence due to the increasing prevalence of antibiotic-resistant Gram-negative infections, highlighting a need for new therapeutic strategies. Studies have shown that LptA interacts with other proteins in the LPS transport pathway, indicating a complex network of interactions that are vital for bacterial survival. The recombinant expression of LptA offers a promising avenue for understanding its structural and functional characteristics, as well as its role in Gram-negative pathogenesis. Moreover, insights gained from LptA studies may contribute to the development of novel antibiotics targeting LPS biosynthesis and transport, potentially overcoming resistance mechanisms. Investigations into LptA's structure through techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy are crucial for elucidating its function and guiding drug design. Overall, the study of LptA and its recombinant forms is integral to advancing our understanding of bacterial physiology and developing effective antimicrobial agents to combat resistant pathogens.
