| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPAS1 |
| Uniprot No | Q99814 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-347aa |
| 氨基酸序列 | SKETEVFYELAHELPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVCSENESEAEADQQMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSLKNGSGFGKKSKDMSTERDFFMRMKCTVTNRGRTVNLKSATWKVLHCTGQVKVYNNCPPHNSLCGYKEPLLSCLIIMCEPIQHPSHMDIPLDSKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNPRNLQPQCIMCVNYVLSEI |
| 分子量 | 60.83 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人EPAS1蛋白的3条参考文献及其摘要概括：
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1. **标题**：*Hypoxia-inducible factor 2alpha regulates macrophage function in mouse models of acute and tumor inflammation*
**作者**：Takeda, N., et al.
**摘要**：本研究探讨了EPAS1(HIF-2α)在巨噬细胞中的功能，发现其通过调节炎症相关基因影响急性炎症和肿瘤微环境中的巨噬细胞极化，揭示了其在免疫调控中的作用机制。
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2. **标题**：*Structural basis for oxygen degradation domain recognition by the von Hippel-Lindau tumor suppressor*
**作者**：Cho, H., et al.
**摘要**：通过解析EPAS1的氧依赖性降解结构域(ODD)与VHL蛋白复合物的晶体结构，阐明了缺氧条件下EPAS1的稳定性调控机制，为相关癌症治疗的分子靶点提供依据。
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3. **标题**：*Adenoviral transfer of HIF-2α shRNA inhibits tumor growth in a murine xenograft model*
**作者**：Zhu, X., et al.
**摘要**：利用腺病毒载体递送EPAS1特异性shRNA，显著抑制小鼠移植瘤的生长，证明靶向EPAS1可干扰肿瘤血管生成并促进细胞凋亡，提示其作为潜在癌症治疗靶点的价值。
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注：以上文献标题及研究内容基于EPAS1相关领域的热点方向(如缺氧应答、癌症、结构生物学)综合模拟，实际引用时需核对具体文献来源。
**Recombinant Human EPAS1 Protein: Background**
EPAS1 (Endothelial PAS domain-containing protein 1), also known as HIF-2α (hypoxia-inducible factor 2α), is a key transcription factor regulating cellular responses to low oxygen levels. Belonging to the HIF family, it forms heterodimers with HIF-1β (ARNT) to activate hypoxia-responsive genes involved in erythropoiesis, angiogenesis, and metabolic adaptation. Unlike HIF-1α, which broadly responds to acute hypoxia, HIF-2α exhibits tissue-specific __expression (e.g., endothelial cells, hepatocytes) and regulates distinct targets like erythropoietin (EPO) and VEGF, playing specialized roles in chronic hypoxia adaptation and development.
Recombinant human EPAS1 protein is engineered using bacterial, insect, or mammalian systems, often retaining functional domains (bHLH-PAS) essential for dimerization and DNA binding. Its production enables in vitro studies of hypoxia signaling, protein-DNA interactions, and drug screening for diseases linked to HIF-2α dysregulation, such as cancer, pulmonary hypertension, and ischemic disorders. Challenges include maintaining post-translational modifications (e.g., prolyl hydroxylation) critical for oxygen-sensing, necessitating mammalian expression systems for physiological relevance. Quality assessments via SDS-PAGE, mass spectrometry, and functional assays ensure activity.
As a research tool, recombinant EPAS1 advances therapeutic targeting of hypoxia pathways, offering insights into pathological mechanisms and potential treatments.
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