Analytical Data
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Gene name
monooxygenase
- Application
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Alternative Names
Renilla-type luciferase
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Species
Renilla reniformis
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27652
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Expression Region
1-311aa
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Molecular Weight
56 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
Monooxygenases are a class of enzymes that play crucial roles in various biological processes by catalyzing the incorporation of one atom of oxygen from molecular oxygen (O2) into organic substrates while reducing the second oxygen atom to water (H2O). This unique oxidative capability enables monooxygenases to participate in the metabolism of a wide range of compounds, including pharmaceuticals, environmental pollutants, and biomolecules. Their importance in bioremediation and synthetic biology has led to a significant interest in the recombinant production of monooxygenases, which allows for the study of these enzymes in detail and their application in various industrial processes. Utilizing recombinant DNA technology, researchers can produce these enzymes in host organisms, such as bacteria or yeast, and manipulate their genetic sequences to improve stability, activity, and substrate specificity. The study of recombinant monooxygenases is essential for understanding metabolic pathways, developing environmentally friendly biocatalysts, and designing novel biocatalytic processes for chemical synthesis. This area of research holds promise for the advancement of sustainable technologies and the development of new therapeutic agents, highlighting the continuous need for innovation and exploration in enzymology and biotechnology. As the field progresses, structural biology, protein engineering, and high-throughput screening methods are increasingly utilized to optimize the characteristics and functional properties of monooxygenases, paving the way for new applications in green chemistry and bioprocessing.
