Analytical Data
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Gene name
oxidase
- Application
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Alternative Names
Germin
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Species
Hordeum vulgare
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P45850
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Expression Region
1-201aa
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Molecular Weight
28.2 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
Oxidases are a class of enzymes that catalyze the transfer of electrons from substrates to oxygen, resulting in the production of hydrogen peroxide or other reactive oxygen species. These enzymes play crucial roles in various biological processes, including cellular respiration, metabolism, and signal transduction. The study of oxidases has garnered considerable interest due to their potential applications in biotechnology and medicine, such as in biosensors, biofuel cells, and therapeutic agents for oxidative stress-related diseases. Recombinant protein technology has enabled researchers to produce oxidases in a controlled manner, allowing for detailed studies of their structure, function, and mechanism. By utilizing techniques such as genetic engineering and protein expression systems, scientists can optimize these enzymes for specific applications, enhancing their stability, activity, and substrate specificity. Furthermore, understanding the molecular basis of oxidase activity can lead to the development of inhibitors that may serve as drugs for combating oxidative damage in cells. Overall, research on recombinant oxidases is paving the way for innovative solutions in both environmental and health-related fields, highlighting the importance of these enzymes in science and industry.
