Analytical Data
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Gene name
lasA
- Application
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Alternative Names
Staphylolytic protease
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Species
Pseudomonas aeruginosa
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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
P14789
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Expression Region
237-418aa
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Molecular Weight
36 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
LasA is a crucial virulence factor produced by the pathogenic bacterium Pseudomonas aeruginosa, which is known for causing severe infections, particularly in immunocompromised individuals and those with chronic lung diseases like cystic fibrosis. Research into LasA has garnered significant attention due to its role in degrading extracellular matrix components, thereby facilitating bacterial invasion and biofilm formation. Understanding the structural and functional properties of LasA is essential for developing potential therapeutic strategies to combat P. aeruginosa infections. Recent studies have focused on the recombinant expression of LasA to elucidate its enzymatic mechanisms and identify possible inhibitors. Advances in recombinant protein technology have allowed for the production of large quantities of LasA in heterologous systems, providing a platform for biochemical assays and structural analysis. This research not only enhances our comprehension of LasA's biological role but also paves the way for novel antimicrobial agents that can target its activity. To date, various studies have characterized the enzymatic activity of LasA and its interactions with host tissues, underscoring its importance in P. aeruginosa's pathogenesis.
