Analytical Data
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Gene name
lecA
- Application
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Alternative Names
Galactose-binding lectin
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Species
Pseudomonas aeruginosa
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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
Q05097
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Expression Region
2-122aa
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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, a lectin protein originally derived from the pathogen Pseudomonas aeruginosa, has garnered considerable attention in biomedical research due to its significant role in bacterial adhesion, host cell recognition, and biofilm formation. Recognized for its ability to bind specific carbohydrates, LecA participates in the pathogenesis of various infections, making it a potential target for therapeutic interventions. Researchers have focused on recombinant LecA for its utility in various applications, including drug delivery and vaccine development. Understanding the structure-function relationship of LecA has enabled scientists to manipulate its properties for enhanced performance. By producing LecA as a recombinant protein, researchers aim to elucidate its binding mechanisms and explore its potential as an adjuvant in vaccine formulations, ultimately contributing to the design of novel strategies to combat Pseudomonas aeruginosa infections. Additionally, studying LecA offers insights into the broader field of glycoengineering and glycoprotein interactions, highlighting the importance of carbohydrate recognition in microbial pathogenesis and immune responses.
