| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EGLN2 |
| Uniprot No | Q96KS0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 283-407aa |
| 氨基酸序列 | MVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT |
| 预测分子量 | 32.3 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EGLN2重组蛋白的3篇参考文献示例(注：内容为模拟，实际文献需通过学术数据库核实)：
1. **文献名称**: *"Expression and functional characterization of recombinant human EGLN2/PHD1 protein"*
**作者**: Smith A, et al.
**摘要**: 该研究报道了在大肠杆菌中成功表达并纯化具有生物活性的重组人EGLN2蛋白，证实其在体外可特异性羟化HIF-1α的脯氨酸残基，依赖铁离子和抗坏血酸辅因子。
2. **文献名称**: *"Structural insights into EGLN2-mediated oxygen sensing by crystallographic analysis"*
**作者**: Lee JH, et al.
**摘要**: 通过X射线晶体学解析重组EGLN2蛋白的三维结构，揭示其底物结合口袋的关键氨基酸残基，为设计靶向EGLN2的小分子抑制剂提供了结构基础。
3. **文献名称**: *"EGLN2 recombinant protein suppresses tumor growth via HIF pathway modulation in a xenograft model"*
**作者**: Zhang Y, et al.
**摘要**: 利用重组EGLN2蛋白处理肿瘤细胞，发现其通过降解HIF-1α抑制血管生成基因表达，在动物模型中显著延缓肿瘤生长，提示其潜在治疗应用价值。
建议通过PubMed或Web of Science以 **"EGLN2 recombinant protein"** 或 **"PHD1 protein purification"** 为关键词检索最新文献获取准确信息。
EGLN2. also known as prolyl hydroxylase domain-containing protein 2 (PHD2), is a critical oxygen-sensing enzyme belonging to the α-ketoglutarate-dependent dioxygenase family. It plays a central role in regulating cellular responses to hypoxia by targeting hypoxia-inducible factor alpha (HIF-α) subunits for degradation under normoxic conditions. By hydroxylating specific proline residues on HIF-α, EGLN2 promotes its recognition by the von Hippel-Lindau (VHL) E3 ubiquitin ligase complex, leading to proteasomal degradation. This process is essential for maintaining oxygen homeostasis, angiogenesis, and metabolic adaptation.
Recombinant EGLN2 protein is produced in vitro using expression systems like *E. coli* or mammalian cells, enabling researchers to study its biochemical properties, enzymatic activity, and interactions with substrates or inhibitors. The purified protein typically retains hydroxylase activity, allowing in vitro assays to investigate oxygen-dependent regulation of HIF pathways. Structurally, it contains conserved Fe²⁺- and α-ketoglutarate-binding domains critical for catalysis.
Research applications include exploring its role in diseases linked to hypoxia signaling, such as cancer, ischemic disorders, and anemia. EGLN2 inhibitors are being investigated for therapeutic use in anemia by stabilizing HIF and stimulating erythropoietin production. Conversely, its overexpression in some cancers highlights its potential as a drug target. Recombinant EGLN2 also aids in studying non-HIF substrates, including proteins involved in metabolism and inflammation, broadening its relevance in cellular physiology and disease mechanisms. Its versatility makes it a key tool for hypoxia-related biomedical research.
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