Analytical Data
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基因名
dioxygenase
- Application
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别名
Catechol 1,2-dioxygenase; EC 1.13.11.1; Fragment
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种属
Acinetobacter calcoaceticus
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表达系统
E. coli
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标签
N- His-SUMO & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P83715
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表达区间
1-14aa
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分子量
21.7 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.












