Analytical Data
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Gene name
plyA
- Application
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Alternative Names
plyA；Pectate lyase A
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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
B8NE46
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Expression Region
21-321aa
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AA Sequence
APTKTIGKRAAITDVAHGYASQNGGTTGGAGGTTTTVSSYAQFTEAVSSDDAKIVIVDGTITETADQVKVGSNTSIIGKDANAILEGFGLLVKEKENVIIRNLGVKKVLADNGDAIGVQYSNNVWIDHCDVSSDRDHDKDYYDGLIDLTHAADYVTVSNTFVHDHWKAMLFGHSDSNGDEDTGHLRITVNNNYLNNLNSRGPSFRFGTGHLYNNYYLDVSDGINTRQGAQLLVEGNVWSGGKKPLYSTDDGYAVARDNDFGDGENTAPEGTLTSVPYEYDLLAASAVKDAVVGTAGQTLTF
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Molecular Weight
36.2 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
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Protein Description
The study of plyA recombinant protein primarily focuses on its role in various biotechnological applications, particularly in the fields of molecular biology and microbiology. PlyA, a bacteriophage-derived endolysin, exhibits potent antibacterial properties by degrading the peptidoglycan layer of bacterial cell walls. This characteristic makes it a promising candidate for the development of novel antimicrobial agents, especially in the face of rising antibiotic resistance. Researchers are exploring the genetic and biochemical properties of plyA to better understand its mechanism of action and to enhance its efficacy by recombinant protein engineering. By incorporating techniques such as gene cloning, expression systems, and purification methods, scientists aim to produce plyA in sufficient quantities for therapeutic use. Additionally, there is growing interest in its potential use as a food preservative due to its specificity against certain pathogenic bacteria, providing a safer alternative to traditional preservatives. Overall, the investigation of plyA recombinant protein not only aims to address pressing health concerns but also opens avenues for innovative solutions in food safety and biomedicine.
