Analytical Data
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Gene name
pylS
- Application
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Alternative Names
Pyrrolysine--tRNA(Pyl) ligase Pyrrolysyl-tRNA synthetase
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Species
Methanosarcina barkeri
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q46E77
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Expression Region
1-419aa
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Molecular Weight
51.8 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 pylS recombinant protein has gained significant attention due to its potential applications in biotechnology and synthetic biology. PylS is a crucial component of the pyrrolysine incorporation machinery, which allows for the inclusion of the 22nd amino acid, pyrrolysine, into proteins during translation. This unique ability expands the genetic code and enables the design of proteins with novel functionalities, offering insights into protein engineering and functional diversity. Research into pylS focuses on understanding its mechanism of action, optimizing its expression in various host organisms, and exploring its interactions with other components of the translational machinery. The successful application of pylS in synthesizing proteins with non-canonical amino acids opens new avenues for drug development, enzyme design, and the creation of advanced biomaterials. Consequently, the investigation of pylS recombinant protein is not only pivotal for fundamental science but also holds promising implications for industrial and therapeutic advancements.
