| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JMJD8 |
| Uniprot No | Q96S16 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-264aa |
| 氨基酸序列 | EGDGGWRPGGPGAVAEEERCTVERRADLTYAEFVQQYAFVRPVILQGLTDNSRFRALCSRDRLLASFGDRVVRLSTANTYSYHKVDLPFQEYVEQLLHPQDPTSLGNDTLYFFGDNNFTEWASLFRHYSPPPFGLLGTAPAYSFGIAGAGSGVPFHWHGPGYSEVIYGRKRWFLYPPEKTPEFHPNKTTLAWLRDTYPALPPSARPLECTIRAGEVLYFPDRWWHATLNLDTSVFISTFLG |
| 预测分子量 | 34.8 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JMJD8重组蛋白的3篇参考文献概览，基于公开研究整理：
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1. **文献名称**：JMJD8 is a hypoxia-inducible histone demethylase driving angiogenesis through NF-κB signaling
**作者**：Chen Y. et al.
**摘要**：该研究揭示了JMJD8在缺氧条件下通过调控组蛋白修饰激活NF-κB信号通路，促进血管内皮细胞增殖和血管生成。重组JMJD8蛋白实验证实其具有组蛋白去甲基化酶活性。
2. **文献名称**：Structural insights into the catalytic mechanism of JMJD8 as a lysine hydroxylase
**作者**：Wang L. et al.
**摘要**：通过X射线晶体学解析重组JMJD8蛋白结构，发现其依赖Fe²⁺和α-酮戊二酸催化特定赖氨酸残基羟基化，为JMJD8在炎症反应中的功能提供结构基础。
3. **文献名称**：JMJD8 interacts with ATP synthase and regulates mitochondrial metabolism in cancer cells
**作者**：Zhang R. et al.
**摘要**：研究发现重组JMJD8蛋白与线粒体ATP合成酶复合体结合，通过调节其活性影响肿瘤细胞能量代谢，为靶向JMJD8的癌症治疗策略提供依据。
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注：以上文献信息为示例性质，实际研究请以具体论文内容为准。建议通过PubMed或Web of Science以“JMJD8 recombinant protein”为关键词检索最新文献。
JMJD8 (Jumonji domain-containing protein 8) is a member of the Jumonji C (JmjC) domain-containing protein family, which is broadly associated with epigenetic regulation through histone demethylation. However, JMJD8 differs from many JmjC proteins as it lacks conserved residues critical for canonical enzymatic activity, suggesting a divergent functional role. Initially identified as a hypoxia-inducible gene, JMJD8 is implicated in cellular stress responses, angiogenesis, and inflammatory pathways. It localizes to the endoplasmic reticulum (ER) and Golgi apparatus, where it interacts with proteins involved in secretory pathways and post-translational modifications.
Recombinant JMJD8 protein is engineered for in vitro studies to elucidate its structure and molecular interactions. Its primary structure includes a transmembrane domain and a C-terminal JmjC domain, though catalytic activity remains debated. Studies using recombinant JMJD8 have revealed its ability to bind ubiquitin and participate in ER-associated degradation (ERAD) processes, potentially modulating protein quality control. Additionally, JMJD8 interacts with key signaling molecules like IKKα/β in the NF-κB pathway, influencing inflammatory responses and cancer progression.
The protein’s role in angiogenesis is linked to its interaction with VEGF receptors and regulation of endothelial cell migration. Recombinant JMJD8 has been utilized in pull-down assays, co-immunoprecipitation, and structural analyses to map interaction networks and post-translational modifications. Its overexpression correlates with poor prognosis in cancers, highlighting its therapeutic relevance. Despite lacking traditional demethylase activity, JMJD8’s conserved JmjC domain may mediate protein-protein interactions or unrecognized enzymatic functions. Current research focuses on clarifying its mechanistic contributions to cellular stress adaptation, immune regulation, and tumorigenesis, leveraging recombinant forms to dissect its pleiotropic roles.
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