Analytical Data
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Gene name
LapB
- Application
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Alternative Names
lapB; yciM; b1280; JW1272; Lipopolysaccharide assembly protein B; Lipopolysaccharide regulatory protein
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0AB58
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Expression Region
17-389aa
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Molecular Weight
58.8 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
LapB is a crucial protein involved in bacterial adhesion and biofilm formation, primarily studied in the context of Pseudomonas aeruginosa and other opportunistic pathogens. It plays a significant role in the bacteria's ability to adhere to surfaces and form structured communities, contributing to its virulence and resistance to antibiotics. Biofilms, which consist of densely packed bacterial cells encased in a self-produced extracellular matrix, pose a major challenge in clinical settings as they can lead to chronic infections and are difficult to eradicate. Understanding the biochemical properties and mechanisms of LapB, including its role in cell-surface interactions and its regulatory pathways, is essential for developing new therapeutic strategies to combat biofilm-associated infections. Recent studies have employed various techniques, such as molecular cloning, protein purification, and functional assays, to elucidate the structure-function relationship of LapB and its interactions with other cellular components. Investigating LapB's potential as a target for antibacterial drug development could pave the way for innovative approaches to manage persistent infections caused by biofilm-forming bacteria.
