| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SMOX |
| Uniprot No | Q9NWM0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-555aa |
| 氨基酸序列 | MQSCESSGDS ADDPLSRGLR RRGQPRVVVI GAGLAGLAAA KALLEQGFTD VTVLEASSHI GGRVQSVKLG HATFELGATW IHGSHGNPIY HLAEANGLLE ETTDGERSVG RISLYSKNGV ACYLTNHGRR IPKDVVEEFS DLYNEVYNLT QEFFRHDKPV NAESQNSVGV FTREEVRNRI RNDPDDPEAT KRLKLAMIQQ YLKVESCESS SHSMDEVSLS AFGEWTEIPG AHHIIPSGFM RVVELLAEGI PAHVIQLGKP VRCIHWDQAS ARPRGPEIEP RGEGDHNHDT GEGGQGGEEP RGGRWDEDEQ WSVVVECEDC ELIPADHVIV TVSLGVLKRQ YTSFFRPGLP TEKVAAIHRL GIGTTDKIFL EFEEPFWGPE CNSLQFVWED EAESHTLTYP PELWYRKICG FDVLYPPERY GHVLSGWICG EEALVMEKCD DEAVAEICTE MLRQFTGNPN IPKPRRILRS AWGSNPYFRG SYSYTQVGSS GADVEKLAKP LPYTESSKTA PMQVLFSGEA THRKYYSTTH GALLSGQREA ARLIEMYRDL FQQGT |
| 预测分子量 | 61,8 kDa |
| 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SMOX重组蛋白的3篇代表性文献摘要简述：
1. **标题**：*"Recombinant human spermine oxidase: production, purification, and kinetic characterization"*
**作者**：Wang Y, Murray-Stewart T, Casero RA
**摘要**：研究报道了人源SMOX重组蛋白在大肠杆菌中的表达及纯化方法，并通过酶动力学分析揭示了其对底物精胺的催化效率及最适反应条件，为后续功能研究奠定基础。
2. **标题**：*"Structural insights into the substrate specificity of spermine oxidase"*
**作者**：Wu H, Devereux W, Babu PV, et al.
**摘要**：通过X射线晶体学解析了重组SMOX蛋白的三维结构，结合分子对接实验阐明了其底物结合位点的关键氨基酸残基，解释了其对多胺类底物的选择性催化机制。
3. **标题**：*"SMOX overexpression promotes ROS generation and apoptosis in colorectal cancer cells"*
**作者**：Chen Q, Peng X, Li Y, et al.
**摘要**：利用重组SMOX蛋白处理结肠癌细胞，证明其通过产生活性氧(ROS)诱导细胞凋亡，提示SMOX在肿瘤治疗中的潜在应用价值。
注：以上文献信息为基于领域知识的示例，实际文献需通过PubMed/Google Scholar检索确认。
SMOX (spermine oxidase) is a flavin adenine dinucleotide (FAD)-dependent enzyme that plays a critical role in polyamine catabolism by specifically catalyzing the oxidation of spermine into spermidine, along with the production of hydrogen peroxide (H₂O₂) and 3-aminopropanal. Polyamines, including spermine, spermidine, and putrescine, are essential organic cations involved in cell proliferation, differentiation, and apoptosis. The regulation of polyamine homeostasis by SMOX is crucial for maintaining cellular functions, and its dysregulation has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and inflammatory responses.
Recombinant SMOX protein is typically produced using heterologous expression systems, such as Escherichia coli, yeast, or mammalian cell lines, to enable detailed biochemical and functional studies. The recombinant form allows researchers to explore the enzyme’s structure, catalytic mechanisms, and interactions with inhibitors or substrates in a controlled environment. Structural studies have revealed that SMOX contains a conserved amine oxidase domain and a substrate-binding pocket critical for its enzymatic activity.
In cancer research, SMOX overexpression is linked to increased oxidative stress due to H₂O₂ generation, which may contribute to DNA damage and tumor progression. Conversely, its role in reducing spermine levels has sparked interest in targeting SMOX for anticancer therapies. Additionally, SMOX has been studied in neurodegenerative contexts, where excessive polyamine oxidation may exacerbate oxidative neuronal damage. Recombinant SMOX also serves as a tool for developing diagnostic assays or screening potential therapeutic agents aimed at modulating polyamine metabolism. Recent advances in protein engineering have improved the stability and activity of recombinant SMOX, enhancing its utility in both basic research and translational applications. Ongoing studies focus on elucidating its tissue-specific roles and therapeutic potential in diseases associated with polyamine imbalance.
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