Analytical Data
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Gene name
ply
- Application
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Alternative Names
ply；Pneumolysin
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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
P0C2J9
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Expression Region
2-471aa
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AA Sequence
ANKAVNDFILAMNYDKKKLLTHQGESIENRFIKEGNQLPDEFVVIERKKRSLSTNTSDISVTATNDSRLYPGALLVVDETLLENNPTLLAVDRAPMTYSIDLPGLASSDSFLQVEDPSNSSVRGAVNDLLAKWHQDYGQVNNVPARMQYEKITAHSMEQLKVKFGSDFEKTGNSLDIDFNSVHSGEKQIQIVNFKQIYYTVSVDAVKNPGDVFQDTVTVEDLKQRGISAERPLVYISSVAYGRQVYLKLETTSKSDEVEAAFEALIKGVKVAPQTEWKQILDNTEVKAVILGGDPSSGARVVTGKVDMVEDLIQEGSRFTADHPGLPISYTTSFLRDNVVATFQNSTDYVETKVTAYRNGDLLLDHSGAYVAQYYITWNELSYDHQGKEVLTPKAWDRNGQDLTAHFTTSIPLKGNVRNLSVKIRECTGLAWEWWRTVYEKTDLPLVRKRTISIWGTTLYPQVEDKVEND
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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 (plyopathic) recombinant proteins has gained significant attention due to their potential applications in biotechnology and medicine. Ply proteins are derived from bacteriophage lysins, which are enzymes that can degrade bacterial cell walls. As antibiotic resistance poses a growing threat to public health, researchers have turned to alternative strategies for combating bacterial infections. Ply proteins, particularly those designed to target specific pathogenic bacteria, offer a promising avenue for the development of new antimicrobial agents. These proteins can selectively lyse targeted bacterial cells without harming human cells, making them attractive candidates for therapeutic interventions. Additionally, the recombinant technology allows the engineering of ply proteins to enhance their efficacy, stability, and spectrum of activity. Recent advances in genetic engineering and protein design are paving the way for tailored ply recombinants, which can be utilized in various fields, including food safety, clinical diagnostics, and bioengineering. As research progresses, understanding the structure-function relationships of these proteins is crucial for optimizing their performance and expanding their applications. Overall, the exploration of ply recombinant proteins represents a cutting-edge frontier in the fight against antibiotic-resistant bacteria and holds the promise of innovative solutions in microbial control and infection management.
