Analytical Data
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Gene name
lasA
- Application
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Alternative Names
lasA；PRKACN1；cAMP-dependent Protein kinase inhibitor alpha
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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
P23826
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Expression Region
32-68aa
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AA Sequence
STPVLASVA VSMELLPTAS VLYSDVAGCF KYSAKHHC
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Molecular Weight
7.2 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 lysin derived from Pseudomonas aeruginosa, a significant opportunistic pathogen associated with various infections, especially in immunocompromised individuals. Understanding LasA and its recombinant forms has garnered substantial attention due to its potential therapeutic applications, particularly in combating antibiotic-resistant bacterial strains. Research on LasA has focused on its role in bacterial cell wall lysis, as it exhibits endopeptidase activity that specifically targets the peptidoglycan layer, promoting cell death in Gram-positive bacteria. Recombinant protein technology has enabled the production of LasA in heterologous systems, facilitating detailed studies of its structure-function relationships and enhancing its potential application in biomedicine. The ability to engineer LasA variants with improved stability and efficacy has opened avenues for developing novel antimicrobial agents, offering alternative treatment strategies against P. aeruginosa infections and other resistant pathogens. Additionally, understanding the mechanisms by which LasA interacts with bacterial cell walls contributes to the broader field of antibacterial drug development and resistance mitigation. Overall, the research on LasA recombinant proteins stands at the intersection of microbiology, biochemistry, and therapeutic development, addressing the urgent need for new antimicrobial solutions in the face of rising resistance challenges.
