Analytical Data
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Gene name
LUXS
- Application
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Alternative Names
AI-2 synthesis protein;Autoinducer-2 production protein LuxS
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P45578
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Expression Region
2-171aa
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Molecular Weight
23.3 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
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Protein Description
LUXS (Lethal Underexpression of X-linked Gene 1) is a crucial enzyme that plays a significant role in the biosynthesis of autoinducer-2 (AI-2), a signaling molecule involved in bacterial communication through quorum sensing. Quorum sensing is a critical mechanism that allows bacteria to coordinate their behavior in response to population density, affecting processes such as biofilm formation, virulence, and bioluminescence. The importance of LUXS in this physiological context has spurred interest in understanding its molecular structure, enzymatic functions, and regulation. Additionally, research has explored the potential of LUXS as a target for antimicrobial therapies, as inhibiting its function could disrupt bacterial communication and virulence. By studying the structural and functional properties of LUXS, scientists aim to identify novel inhibitors that could serve as effective treatments against pathogenic bacteria, particularly those that employ quorum sensing to enhance their virulence. The elucidation of LUXS's mechanisms is not only pivotal for developing new antimicrobial strategies but also for advancing our understanding of microbial ecology and the intricate interactions within microbial communities. As antibiotic resistance becomes a growing concern, research on LUXS and its role in bacterial signaling presents an exciting avenue for innovative therapeutic approaches, reinforcing the need for continued investigation into this enzyme's properties and its broader implications in microbiology.
