Analytical Data
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Gene name
lecA
- Application
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Alternative Names
lecA；KIAA0973；SAST；Microtubule-associated serine/threonine-Protein kinase 1
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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
Q05097
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Expression Region
2-122aa
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AA Sequence
AWKGEVLANNEAGQVTSIIYNPGDVITIVAAGWASYGPTQKWGPQGDREHPDQGLICHDAFCGALVMKIGNSGTIPVNTGLFRWVAPNNVQGAITLIYNDVPGTYGNNSGSFSVNIGKDQS
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Molecular Weight
16.8 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
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Protein Description
LecA is a lectin protein derived from the pathogenic bacterium Pseudomonas aeruginosa, which plays a significant role in the organism's ability to adhere to and invade host tissues. This protein specifically binds to galactosides, a property that facilitates bacterial colonization and enhances virulence in infections, particularly in immunocompromised individuals. Research into LecA has gained prominence due to its potential as a target for therapeutic interventions, particularly in developing novel anti-adhesive strategies to combat bacterial infections. Understanding the molecular mechanisms of LecA's interactions with host cells is crucial for designing new antimicrobial agents or preventive measures against P. aeruginosa infections, which are notoriously difficult to treat due to antibiotic resistance. Additionally, LecA's unique properties make it a candidate for use in drug delivery systems and as a biomarker in diagnostic tools. Recent studies have focused on characterizing LecA's structural features, binding affinities, and the signaling pathways activated upon its interaction with host cells. As the global threat of antibiotic-resistant pathogens continues to escalate, LecA and its recombinant forms represent a promising area of research, offering insights into potential interventions that could mitigate the impact of infections caused by this versatile and opportunistic pathogen.
