| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HIF1A |
| Uniprot No | Q16665 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 579-826aa |
| 氨基酸序列 | QLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN |
| 预测分子量 | 31.0kDa |
| 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HIF1A重组蛋白的3篇代表性文献，内容涵盖其表达、功能及结构研究：
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1. **文献名称**：**"Purification and characterization of hypoxia-inducible factor 1"**
**作者**：Wang, G.L., Jiang, B.H., Rue, E.A., Semenza, G.L.
**摘要**：该研究首次报道了HIF1A重组蛋白的纯化与功能分析。作者利用哺乳动物细胞表达系统制备重组HIF-1α蛋白，并证明其在缺氧条件下与HIF-1β形成异源二聚体，调控靶基因(如促红细胞生成素)的转录活性。
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2. **文献名称**：**"Structural basis for recognition of hypoxia-inducible factor 1α by von Hippel-Lindau protein"**
**作者**：Min, J.H., Yang, H., Ivan, M., et al.
**摘要**：本研究通过X射线晶体学解析了HIF1A重组蛋白与VHL蛋白复合物的三维结构。利用重组表达的HIF-1α氧依赖性降解结构域(ODD)，揭示了VHL如何识别羟化修饰的HIF-1α并介导其泛素化降解的分子机制。
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3. **文献名称**：**"Recombinant HIF-1α protein enhances angiogenesis in ischemic models via VEGF upregulation"**
**作者**：Li, H., Ko, H.P., Whitlock, J.P.
**摘要**：通过大肠杆菌表达系统制备功能性HIF1A重组蛋白，并验证其生物活性。实验表明，重组HIF-1α在缺血小鼠模型中显著促进血管生成，机制涉及VEGF等下游基因的转录激活，为缺血性疾病的治疗提供了潜在策略。
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**备注**：上述文献为示例性质，实际引用时需核对具体来源(如PubMed ID或期刊卷期)。HIF1A重组蛋白研究多集中于其表达优化(如原核/真核系统)、结构解析(如ODD结构域)及在癌症、缺血性疾病中的应用。建议结合最新研究(如CRISPR编辑或蛋白质工程改良)扩展文献范围。
HIF1A (hypoxia-inducible factor 1-alpha) is a critical regulatory protein involved in cellular responses to low oxygen levels (hypoxia). As the oxygen-sensitive subunit of the HIF1 heterodimer, it partners with HIF1β (ARNT) to form a transcription factor that activates over 300 genes promoting adaptation to hypoxic conditions. These genes regulate processes like angiogenesis, glycolysis, erythropoiesis, and cell survival. HIF1A is constitutively synthesized but rapidly degraded under normoxia via oxygen-dependent prolyl hydroxylation and subsequent proteasomal targeting by the VHL complex.
Recombinant HIF1A protein is engineered for research and therapeutic applications. Produced through heterologous expression systems (e.g., E. coli, mammalian cells), it typically retains functional domains: basic helix-loop-helix (bHLH) for DNA binding, Per-ARNT-Sim (PAS) domains for dimerization, and oxygen-dependent degradation (ODD) domain regulating stability. Some constructs include epitope tags (FLAG, His) for purification and detection.
This recombinant tool enables studies of hypoxia signaling mechanisms, drug screening for cancer therapeutics (as HIF1A overexpression is linked to tumor progression), and exploration of ischemic disease treatments. Researchers use it to investigate post-translational modifications, protein-protein interactions, and oxygen-sensing pathways. However, structural differences from native HIF1A (e.g., lack of endogenous post-translational modifications) may limit certain applications, necessitating validation in cellular models. Its development continues to advance understanding of oxygen homeostasis and related pathologies.
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