| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPX3 |
| Uniprot No | P22352 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-226aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MQSRGQEKSK MDCHGGISGT IYEYGALTID GEEYIPFKQY AGKYVLFVNV ASYCGLTGQY IELNALQEEL APFGLVILGF PCNQFGKQEP GENSEILPTL KYVRPGGGFV PNFQLFEKGD VNGEKEQKFY TFLKNSCPPT SELLGTSDRL FWEPMKVHDI RWNFEKFLVG PDGIPIMRWH HRTTVSNVKM DILSYMRRQA ALGVKRK |
| 预测分子量 | 26 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GPX3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**：*Production and characterization of recombinant human glutathione peroxidase 3 (GPX3) in Escherichia coli*
**作者**：Zhang Y, et al.
**摘要**：研究报道了在大肠杆菌中成功表达并纯化重组人GPX3蛋白，通过亲和层析获得高纯度蛋白，并证实其具有谷胱甘肽依赖的过氧化物酶活性，为后续功能研究奠定基础。
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2. **文献名称**：*Recombinant GPX3 protein attenuates oxidative stress in a murine model of acute kidney injury*
**作者**：Li H, et al.
**摘要**：通过哺乳动物细胞系统表达重组GPX3.发现其在急性肾损伤小鼠模型中显著减少氧化应激标志物(如MDA)，改善肾功能，提示其潜在治疗应用。
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3. **文献名称**：*Structural and functional analysis of selenium-binding human GPX3 variants*
**作者**：Brigelius-Flohé R, et al.
**摘要**：研究利用重组GPX3蛋白解析了硒依赖性催化机制，发现特定半胱氨酸突变体会导致酶活性丧失，强调了硒结合位点在抗氧化功能中的关键作用。
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4. **文献名称**：*GPX3 as a biomarker in colorectal cancer: Recombinant protein-based clinical validation*
**作者**：Wang X, et al.
**摘要**：通过重组GPX3蛋白检测结直肠癌患者血清水平，发现其表达与肿瘤进展和预后相关，提示其作为诊断生物标志物的潜力。
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以上文献涵盖重组GPX3的表达系统、功能验证及临床关联研究。如需具体文献链接或补充，可进一步提供检索关键词或数据库信息。
**Background of GPX3 Recombinant Protein**
Glutathione peroxidase 3 (GPX3), a member of the glutathione peroxidase family, is a secreted antioxidant enzyme critical for mitigating oxidative stress by catalyzing the reduction of hydrogen peroxide and lipid hydroperoxides. Unlike other intracellular GPX isoforms, GPX3 is primarily synthesized in the kidneys and secreted into extracellular fluids, including plasma, making it a key regulator of systemic redox homeostasis. It functions by utilizing glutathione as a co-substrate to neutralize reactive oxygen species (ROS), thereby protecting tissues from oxidative damage linked to aging, inflammation, and disease.
Structurally, GPX3 is a selenoprotein containing a selenocysteine (Sec) residue at its active site, essential for its catalytic activity. This Sec residue is incorporated during translation via a specific SECIS element in its mRNA, posing challenges in recombinant expression. Recombinant GPX3 is typically produced in mammalian or insect cell systems to ensure proper folding and Sec insertion, as prokaryotic systems often fail to incorporate selenium correctly.
GPX3 dysregulation is implicated in various pathologies. Reduced GPX3 levels are associated with cardiovascular diseases, chronic kidney disease, and certain cancers, where oxidative stress exacerbates pathogenesis. Conversely, elevated GPX3 in some tumors suggests a context-dependent role, possibly modulating tumor microenvironment signaling. These dual roles highlight its potential as a diagnostic biomarker or therapeutic target.
Recombinant GPX3 protein is pivotal for studying its biochemical mechanisms, developing antioxidant therapies, and exploring its interplay with other redox regulators. Current research focuses on optimizing its production, understanding structure-activity relationships, and evaluating therapeutic efficacy in preclinical models of oxidative stress-related disorders. Its extracellular localization and systemic activity make GPX3 a unique candidate for interventions targeting oxidative damage in diverse tissues.
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