Analytical Data
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Gene name
dioxygenase
- Application
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Alternative Names
Catechol 1,2-dioxygenase; EC 1.13.11.1; Fragment
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Species
Acinetobacter calcoaceticus
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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
P83715
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Expression Region
1-14aa
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Molecular Weight
21.7 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
Dioxygenases are a diverse group of oxygenase enzymes that catalyze the incorporation of molecular oxygen into substrates, playing crucial roles in various biological processes, including the degradation of lignin, the metabolism of aromatic compounds, and the biosynthesis of natural products. Their versatility makes them significant in both ecological and industrial applications, such as bioremediation and the development of pharmaceuticals. The study of recombinant dioxygenases has gained momentum due to advances in genetic engineering and protein expression technologies, enabling the production of these enzymes in manageable quantities for experimental purposes. Researchers are particularly interested in understanding the structure-function relationships of dioxygenases to elucidate their reaction mechanisms and improve their catalytic efficiency. Furthermore, recombinant dioxygenases can serve as valuable tools in synthetic biology, allowing for the preparation of novel compounds through biotransformation processes. The potential for designing engineered dioxygenases with tailored activities opens new avenues for the production of biofuels, specialty chemicals, and environmentally friendly pesticides, highlighting the importance of continued research in this field. Investigating these enzymes through recombinant expression not only enhances our knowledge of their biochemical pathways but also sets the stage for innovative applications that could address pressing environmental challenges and contribute to sustainable development.
