Analytical Data
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Gene name
PLY
- Application
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Alternative Names
Thiol-activated cytolysin
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Species
Streptococcus pneumoniae serotype 4
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Source
E. coli
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Tag
N- His-Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0C2J9
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Expression Region
2-471aa
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Molecular Weight
58.7 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 PLY (Plyolysin) recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including microbiology, biotechnology, and medicine. PLY is a widely studied pore-forming toxin derived from Streptococcus pneumoniae, known for its ability to induce lysis in target cells. Understanding the structure-function relationship of PLY has been pivotal in elucidating its mechanism of action and role in bacterial pathogenesis. Researchers have focused on producing recombinant forms of PLY to explore its properties, improve its safety profile, and harness its capabilities for therapeutic purposes. These include developing PLY-based vaccines and engineering it as a tool for targeted drug delivery or as a diagnostic marker for pneumococcal infections. Furthermore, advancements in protein expression systems have enabled large-scale production of PLY and its variants, facilitating detailed studies on its biochemical properties. As a result, the research on PLY recombinant proteins is not only crucial for understanding bacterial infection mechanisms but also holds promise for innovative biotechnological applications that can benefit human health.
