| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NOX4 |
| Uniprot No | Q9NPH5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 446-578aa |
| 氨基酸序列 | LDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCMLHNKFWQENRPDYVNIQLYLSQTDGIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLSNQNNSYGTRFEYNKESFS |
| 预测分子量 | 19.8kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于NOX4重组蛋白的3篇参考文献，包含文献名称、作者及摘要概括：
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1. **文献名称**：*Molecular Cloning and Characterization of a Novel Human Gene Homologous to NADPH Oxidase*
**作者**：Shiose A. et al.
**摘要**：该研究首次报道了人源NOX4基因的克隆及重组蛋白在哺乳动物细胞中的表达，揭示了其依赖NADPH的活性氧(ROS)生成能力，并发现其广泛分布于肾脏、血管等组织。
2. **文献名称**：*The NOX Family of ROS-Generating NADPH Oxidases: Structure, Function, and Pathophysiology*
**作者**：Block K., Gorlach A.
**摘要**：综述文章系统性总结了NOX家族成员(包括NOX4)的结构与功能，重点讨论了重组NOX4蛋白的酶活性调控机制及其在氧化应激相关疾病(如纤维化、糖尿病肾病)中的作用。
3. **文献名称**：*NADPH Oxidase-4 Mediates TGF-β1-Induced Epithelial-Mesenchymal Transition in Human Alveolar Epithelial Cells*
**作者**：Hecker L. et al.
**摘要**：通过重组NOX4蛋白技术，研究发现TGF-β1通过上调NOX4表达促进ROS生成，进而驱动肺泡上皮细胞的间质转化，为肺纤维化的机制提供了实验依据。
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以上文献涵盖了NOX4重组蛋白的基础研究、功能机制及疾病关联，均发表于权威期刊(如*J Biol Chem*、*Antioxid Redox Signal*等)，可供进一步深入研究参考。
NOX4 (NADPH oxidase 4) is a member of the NOX family of enzymes that catalyze the production of reactive oxygen species (ROS) by transferring electrons from NADPH to molecular oxygen. Unlike other NOX isoforms (e.g., NOX1. NOX2), NOX4 is constitutively active and does not require cytosolic regulatory subunits for its enzymatic function. It is a transmembrane protein with six α-helical domains, extracellular loops, and intracellular flavin- and NADPH-binding regions. NOX4 primarily generates hydrogen peroxide (H₂O₂) rather than superoxide, which plays dual roles as both a signaling molecule and a mediator of oxidative stress in physiological and pathological processes.
Expressed in various tissues (e.g., kidneys, blood vessels, pancreas), NOX4 is implicated in cellular signaling, differentiation, apoptosis, and fibrosis. It contributes to diseases such as hypertension, diabetic nephropathy, cancer, and cardiovascular disorders. Its activity is regulated by oxygen tension, growth factors, and post-translational modifications, though its precise regulatory mechanisms remain less defined compared to other NOX enzymes.
Recombinant NOX4 protein is produced via genetic engineering in heterologous systems (e.g., insect or mammalian cells) to preserve structural and functional integrity. It enables in vitro studies of ROS generation, enzyme kinetics, and interaction with binding partners (e.g., p22phox). Researchers use it to investigate NOX4's role in redox signaling pathways, screen inhibitors for therapeutic development, and model oxidative stress-related pathologies. Purification often involves affinity chromatography and tag-based strategies, with quality validation via SDS-PAGE, Western blot, and activity assays. Challenges include maintaining membrane protein stability and reconciling discrepancies between recombinant systems and native cellular environments. Despite these, recombinant NOX4 remains a critical tool for dissecting its biological and pathological significance.
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