Analytical Data
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Gene name
PF0142
- Application
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Alternative Names
L-asparagine amidohydrolase Cleaved into the following 2 chains: Putative L-asparaginase subunit alpha Putative L-asparaginase subunit beta
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Species
Pyrococcus furiosus
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8U4E6
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Expression Region
1-175aa
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Molecular Weight
35.5 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
PF0142 is a recombinant protein derived from the model organism *Pseudomonas fluorescens*, which has garnered attention due to its potential applications in biotechnology and medicine. The study of PF0142 is motivated by the need for effective antimicrobial agents and biocatalysts, particularly in response to the growing issue of antibiotic resistance and the demands for sustainable industrial processes. Characterizing this protein involves understanding its structure-function relationships, which may reveal mechanisms of action that can be harnessed for drug development or environmental applications. Recent advancements in protein engineering and expression systems have facilitated the production of PF0142 at scale, allowing researchers to explore its biochemical properties and potential use as a biocontrol agent in agriculture. Additionally, elucidating the functional domains of PF0142 could provide insights into novel therapeutic strategies, making it a subject of interest in the fields of microbiology, infectious diseases, and enzymology. As the quest for innovative solutions to modern challenges continues, the research surrounding PF0142 exemplifies the intersection of basic science and practical applications.
