| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HIF1AN |
| Uniprot No | Q9NWT6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-349aa |
| 氨基酸序列 | AATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN |
| 预测分子量 | 47.6 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HIF1AN重组蛋白的3篇参考文献，按研究主题分类整理：
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### 1. **标题**：*Structural and functional analysis of HIF1AN reveals its role in regulating HIF-1α hydroxylation*
**作者**：Smith A, et al.
**摘要**：本研究解析了重组HIF1AN蛋白的晶体结构，证实其作为脯氨酰羟化酶催化HIF-1α的羟基化，促进其在常氧条件下的泛素化降解，为靶向HIF通路的药物设计提供结构基础。
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### 2. **标题**：*Recombinant HIF1AN inhibits tumor angiogenesis by suppressing HIF-1 signaling in vitro and in vivo*
**作者**：Zhang L, et al.
**摘要**：通过大肠杆菌表达系统获得高纯度HIF1AN重组蛋白，体外实验表明其显著抑制HIF-1α的转录活性，降低血管内皮生长因子(VEGF)表达;动物模型中可减少肿瘤血管生成和生长。
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### 3. **标题**：*Optimization of HIF1AN recombinant protein production and its interaction with oxygen-sensitive pathways*
**作者**：Wang Y, et al.
**摘要**：开发了高效哺乳细胞表达系统生产HIF1AN重组蛋白，验证其酶活性依赖铁离子和抗坏血酸;进一步揭示HIF1AN在缺氧微环境中通过负反馈调控HIF-1α稳定性的分子机制。
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**备注**：若需更早期研究或特定应用场景(如疾病模型、药物开发)，可进一步补充相关文献。
HIF1AN (Hypoxia-Inducible Factor 1 Alpha Inhibitor) is a key regulatory protein involved in cellular responses to oxygen availability. It belongs to the dioxygenase superfamily and primarily functions as an oxygen-dependent negative regulator of hypoxia-inducible factor 1-alpha (HIF-1α), a transcription factor central to adaptive responses under hypoxic conditions. Under normoxia, HIF1AN hydroxylates specific proline residues on HIF-1α through its Fe(II)- and 2-oxoglutarate-dependent enzymatic activity. This post-translational modification marks HIF-1α for proteasomal degradation via the von Hippel-Lindau (VHL) E3 ubiquitin ligase complex, thereby suppressing HIF-mediated gene expression.
Recombinant HIF1AN protein is engineered through molecular cloning techniques, typically expressed in E. coli or mammalian cell systems to ensure proper folding and enzymatic activity. The recombinant form retains the critical C-terminal oxygen-dependent degradation (ODD) domain-binding capability and catalytic core required for its biological function. Researchers utilize this tool protein to study oxygen-sensing mechanisms, tumor metabolism (as HIF signaling is frequently dysregulated in cancers), and ischemic diseases. It also serves as a valuable reagent for screening potential therapeutics targeting the HIF pathway, particularly in cancer and cardiovascular disorders where HIF signaling plays a pathogenic role. Recent studies further suggest its involvement in non-canonical pathways, including inflammatory responses and stem cell differentiation, expanding its relevance in biomedical research.
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