| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EGLN3 |
| Uniprot No | Q9H6Z9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-239aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED |
| 预测分子量 | 30 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EGLN3重组蛋白的3篇代表性文献，包含标题、作者及摘要概括：
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1. **标题**: *"Prolyl hydroxylase-3 is the primary oxygen sensor controlling hypoxia-inducible factor-α in renal cells"*
**作者**: Appelhoff RJ et al.
**摘要**: 该研究通过在大肠杆菌中表达并纯化重组EGLN3(PHD3)蛋白，验证其作为氧感受酶对HIF-α亚基的羟化作用，证明其在肾细胞缺氧应答中的核心调控功能。
2. **标题**: *"Structural basis for catalytic activity of the prolyl hydroxylase EGLN3/PHD3"*
**作者**: Chowdhury R et al.
**摘要**: 利用重组EGLN3蛋白进行X射线晶体学分析，解析其与底物及辅因子的复合物结构，揭示其催化HIF-1α羟基化的分子机制及关键活性位点。
3. **标题**: *"EGLN3 inhibition promotes tumor cell apoptosis through HIF-independent mechanisms in glioblastoma"*
**作者**: Lee CM et al.
**摘要**: 研究通过体外表达EGLN3重组蛋白并筛选小分子抑制剂，发现抑制EGLN3可诱导胶质母细胞瘤细胞凋亡，且该效应不依赖HIF通路，提示其潜在治疗价值。
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**注**：若需获取全文或更多文献，建议通过PubMed或Sci-Hub输入标题检索。实际文献可能存在更广泛的研究方向，以上摘要根据典型研究场景概括。
EGLN3 (Egl-9 family hypoxia-inducible factor 3), also known as prolyl hydroxylase domain-containing protein 3 (PHD3), is a member of the EGLN family of oxygen-sensitive prolyl hydroxylases. These enzymes play a critical role in cellular oxygen sensing by regulating the stability of hypoxia-inducible factor (HIF)-α subunits under normoxic conditions. EGLN3 catalyzes the hydroxylation of specific proline residues on HIF-α, marking it for proteasomal degradation via the von Hippel-Lindau (VHL) ubiquitin ligase complex. This process is essential for maintaining oxygen homeostasis and adaptive responses to hypoxia. Unlike other EGLN isoforms (EGLN1/PHD2 and EGLN2/PHD1), EGLN3 exhibits distinct tissue expression patterns, with higher abundance in metabolically active tissues like the heart, brain, and skeletal muscle, suggesting isoform-specific regulatory roles in hypoxia-related pathways.
Recombinant EGLN3 protein is produced through heterologous expression systems (e.g., Escherichia coli or mammalian cells) to enable functional and structural studies. It retains enzymatic activity dependent on iron (Fe²⁺), α-ketoglutarate, and oxygen as cofactors. Researchers utilize this protein to investigate its hydroxylation kinetics, substrate specificity, and interactions with HIF-α or non-canonical targets (e.g., components of apoptosis or metabolic pathways). Its recombinant form is also vital for screening small-molecule inhibitors or activators, with therapeutic potential in diseases linked to HIF dysregulation, such as cancer, ischemic disorders, and chronic kidney disease. Additionally, studies explore EGLN3's role beyond oxygen sensing, including its involvement in mitochondrial function, inflammation, and cell differentiation, highlighting its multifaceted biological significance.
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