Analytical Data
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基因名
NOX5
- Application
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别名
NOX5A; NOX5B; NOX5-A; NOX5-B; NADPH Oxidase,EF-Hand Calcium Binding Domain 5
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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
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q96PH1
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表达区间
Ser456~Phe765
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分子量
40kDa
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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
NOX5 (NADPH oxidase 5) is a member of the NADPH oxidase family, which is crucial for the generation of reactive oxygen species (ROS) in various biological processes. Unlike its other family members, NOX5 is unique due to its calcium-dependent activation mechanism, making it particularly important in cells responsive to calcium fluctuations, such as endothelial cells and certain immune cells. The study of NOX5 has gained significant interest due to its involvement in various pathophysiological conditions, including cardiovascular diseases, cancer, and inflammation. Elevated NOX5 activity has been linked to oxidative stress, contributing to cell signaling dysregulation and tissue damage. Recent advancements in recombinant protein technology have facilitated the production of functional NOX5 proteins, allowing for detailed studies of its enzymatic properties, regulatory mechanisms, and role in ROS-mediated signaling pathways. Understanding the structure and function of NOX5 through recombinant techniques not only sheds light on its biological significance but also provides potential therapeutic insights, as targeting NOX5 could lead to novel treatments for diseases associated with oxidative stress. The elucidation of NOX5's role in cellular processes thus represents a promising avenue for research, with implications for both basic science and clinical applications.
