Analytical Data
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Gene name
plcA
- Application
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Alternative Names
Phosphatidylinositol diacylglycerol-lyase Phosphatidylinositol-specific phospholipase C
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Species
Listeria monocytogenes serovar 1/2a
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P34024
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Expression Region
23-317aa
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Molecular Weight
33.5 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
The study of the PlcA recombinant protein is situated within the broader context of understanding pathogenic mechanisms in bacterial infections, particularly those caused by *Listeria monocytogenes*. PlcA, a phospholipase C, plays a crucial role in the virulence of this bacterium by facilitating cell-to-cell spread through the hydrolysis of phospholipids in host cell membranes. The recombinant expression of PlcA allows researchers to investigate its functional properties, structural characteristics, and interaction with host cells, contributing to a deeper understanding of the invasion strategies employed by this opportunistic pathogen. This research is particularly significant given the rising concerns regarding foodborne diseases and the impact of *Listeria* infections, especially in vulnerable populations such as pregnant women, newborns, and immunocompromised individuals. By characterizing PlcA, scientists aim to identify potential targets for therapeutic intervention and vaccine development. Moreover, this study can enhance our understanding of the molecular mechanisms underpinning bacterial pathogenicity, ultimately leading to improved public health strategies and preventive measures against *Listeria* infections. The exploration of recombinant PlcA not only sheds light on the functional dynamics of this enzyme but also holds promise for the development of novel antimicrobial therapies and better diagnostic tools.
