| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EGLN1 |
| Uniprot No | Q9GZT9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 177-426aa |
| 氨基酸序列 | GGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF |
| 预测分子量 | 35.3 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EGLN1重组蛋白的3篇示例文献(内容为示例性概括，非真实文献)：
1. **"Recombinant Human EGLN1 Protein: Expression, Purification, and Enzymatic Characterization"**
- 作者：Smith J, et al.
- 摘要：研究报道了人源EGLN1重组蛋白在大肠杆菌中的高效表达和纯化方法，通过体外酶活实验验证了其对缺氧诱导因子HIF-1α的羟化活性，并探讨了其依赖α-酮戊二酸和Fe²⁺的催化机制。
2. **"Structural Insights into EGLN1 Recombinant Protein and Its Role in Oxygen Sensing"**
- 作者：Li X, et al.
- 摘要：利用X射线晶体学解析了EGLN1重组蛋白的催化结构域三维结构，揭示了其与底物HIF-1α及小分子抑制剂的结合模式，为靶向EGLN1的药物设计提供了结构基础。
3. **"EGLN1 Recombinant Protein Modulates Erythropoietin Production in Cellular Models of Anemia"**
- 作者：Wang Y, et al.
- 摘要：在细胞模型中验证了重组EGLN1蛋白通过调控HIF-2α稳定性影响促红细胞生成素(EPO)的表达，提示其在治疗贫血相关疾病中的潜在应用价值。
(注：以上文献为示例，实际研究需参考PubMed、Web of Science等数据库的真实文献。)
EGLN1 (Egl-9 family hypoxia-inducible factor 1), also known as prolyl hydroxylase domain-containing protein 2 (PHD2), is a key oxygen-sensing enzyme encoded by the *EGLN1* gene in humans. It belongs to the Fe(II)- and 2-oxoglutarate-dependent dioxygenase family, playing a central role in cellular adaptation to hypoxia by regulating the stability of hypoxia-inducible factor-alpha (HIF-α) subunits. Under normoxic conditions, EGLN1 hydroxylates specific proline residues on HIF-α, marking it for proteasomal degradation via the von Hippel-Lindau (VHL) E3 ubiquitin ligase complex. This process is oxygen-dependent, making EGLN1 a critical mediator of oxygen homeostasis.
Recombinant EGLN1 protein is engineered for in vitro studies and therapeutic development. It is typically produced in heterologous expression systems (e.g., *E. coli* or mammalian cells) to ensure high purity and enzymatic activity. The recombinant protein retains conserved structural features, including the catalytic domain responsible for substrate recognition and hydroxylation. Researchers utilize it to investigate HIF pathway regulation, oxygen-sensing mechanisms, and pathological conditions like cancer, ischemic diseases, and anemia, where HIF signaling is dysregulated.
Pharmaceutical applications focus on developing EGLN inhibitors to stabilize HIF and promote erythropoiesis or angiogenesis. Recombinant EGLN1 serves as a tool for drug screening and mechanistic studies, enabling the design of small molecules (e.g., roxadustat) that modulate its activity. Its role in tumor metabolism and inflammation further underscores its therapeutic relevance. Quality control assays (e.g., hydroxylation activity, kinetic studies) ensure batch consistency for experimental reproducibility.
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