Analytical Data
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基因名
EPHX3
- Application
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别名
(EH3)(Abhydrolase domain-containing protein 9)
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种属
Human
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9H6B9
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表达区间
43-360aa
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分子量
43.9 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
EPHX3, or epoxide hydrolase 3, is an enzyme that plays a crucial role in the metabolism of various xenobiotics and endogenous compounds by catalyzing the conversion of epoxides into their corresponding diols. This enzyme is part of the epoxide hydrolase family, which includes several isoforms with distinct tissue distributions and substrate specificities. Research into EPHX3 has gained attention due to its potential involvement in detoxification processes, inflammatory responses, and disease mechanisms, particularly in the context of cancer and cardiovascular diseases. The understanding of EPHX3’s functional properties and its interaction with various substrates could lead to significant insights into its role in human health and disease. Furthermore, the production of recombinant EPHX3 protein allows for detailed biochemical studies, including kinetic analyses and structural characterization, which are essential for elucidating the enzyme's mechanism and identifying potential inhibitors or activators. This research not only contributes to our fundamental understanding of human metabolism but also holds promise for therapeutic applications, especially in the development of drug-related interventions and personalized medicine strategies. Overall, EPHX3 represents a valuable target for ongoing research due to its multifaceted roles in physiology and pathology, making recombinant protein studies of this enzyme a critical focus in biomedical research.












