Analytical Data
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Gene name
plyC
- Application
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Alternative Names
plyC；Endolysin PlyC. small cell-wall binding subunit
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Species
Human
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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
B0XMA2
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Expression Region
21-420aa
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AA Sequence
LVAFPGAEGFGANAIGGRNGQVYVVTNLNDSGTGSLRDAVSATDRIVVFAVGGVIKISDRIVVSKRVTILGQTAPGDGITVYGNGWSFSNADDAIVRYIRIRMGKGGSSGKDALGIAEGNRMIFDHVSVSWGRDETFSINGDASNITVQNSIIAQGLETHSCGGLMQTDGGVSLFRNLYIDNKTRNPKVKGVNEFTNNVVYNWGGGGGYIAGDSAGQSYANIIGNYFISGPSTSVTAFTRGNANFHGYVQNNYYDPDKDGQLDGFELGVSSSNYGGVAIMSSKYNYPAVAYTMSPAEAVTYVTKYAGASKVRDSVDTQLIAQVQSWGTEGGLISDEATMGGPGTLNGGTPAKDTDGDGIPDEAEKQLGTDPNTNDSMKLHSSGYTYLEVWANSLVPSTYH
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Molecular Weight
49.5 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
PlyC is a phage lysin derived from the bacteriophage C1, known for its ability to lyse specific bacterial strains, particularly those of the Streptococcus genus. As antimicrobial resistance becomes a pressing global health issue, the quest for alternative antibacterial agents has intensified, making PlyC an attractive candidate. This enzyme exhibits a unique mechanism of action by cleaving the peptidoglycan layer of bacterial cell walls, leading to cell lysis. Unlike conventional antibiotics that may target specific bacterial pathways, PlyC shows a broad-spectrum efficacy against various pathogenic strains, including drug-resistant bacteria. Researchers have been focused on the recombinant expression of PlyC to produce it in sufficient quantities for therapeutic applications. Through genetic engineering techniques, scientists have successfully optimized the production of PlyC, enhancing its stability and activity. Studies have shown promising results in using PlyC as a potential treatment for bacterial infections in both clinical and veterinary settings. Furthermore, PlyC's ability to reduce biofilms and resistances further underscores its relevance in modern medicine. Thus, ongoing research aims to better understand PlyC's structure-function relationships, explore its synergistic effects with existing antibiotics, and develop formulations that can effectively deliver this biotherapeutic agent in clinical practice, contributing to combating multi-drug resistant infections.
