Analytical Data
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Gene name
luxS
- Application
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Alternative Names
luxS；ytjB；S-ribosylhomocysteine lyase
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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
C4ZYT7
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Expression Region
1-171aa
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AA Sequence
MPLLDSFTVDHTRMEAPAVRVAKTMNTPHGDAITVFDLRFCVPNKEVMPERGIHTLEHLFAGFMRNHLNGNGVEIIDISPMGCRTGFYMSLIGTPDEQRVADAWKAAMEDVLKVQDQNQIPELNVYQCGTYQMHSLQEAQDIARSILERDVRINSNEELALPKEKLQELHI
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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
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Protein Description
LuxS is a key enzyme involved in the synthesis of autoinducer-2 (AI-2), a signaling molecule that plays a crucial role in bacterial quorum sensing—a process through which bacteria communicate and coordinate their behavior based on population density. The LuxS gene is widely distributed among various bacteria, including both Gram-positive and Gram-negative species, and is implicated in a range of physiological processes such as biofilm formation, virulence, and antibiotic resistance. Research into LuxS and its recombinant protein has gained significant attention due to its potential applications in understanding bacterial social behavior and developing novel antimicrobial strategies. Recombination allows for the expression and purification of LuxS in heterologous systems, enabling detailed biochemical characterization and functional studies. Furthermore, the exploration of LuxS's structure and function could provide insights into the mechanisms of quorum sensing and its evolutionary significance in microbial communities. Investigating LuxS and its role in signaling pathways can shed light on how bacteria adapt to environmental changes, coordinate group behaviors, and contribute to complex microbial ecosystems. Overall, the study of LuxS recombination proteins represents a promising avenue for elucidating fundamental bacterial communication processes and developing innovative therapeutic approaches to combat bacterial infections.
