| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HEBP2 |
| Uniprot No | Q9Y5Z4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-205aa |
| 氨基酸序列 | AEPLQPDPGAAEDAAAQAVETPGWKAPEDAGPQPGSYEIRHYGPAKWVSTSVESMDWDSAIQTGFTKLNSYIQGKNEKEMKIKMTAPVTSYVEPGSGPFSESTITISLYIPSEQQFDPPRPLESDVFIEDRAEMTVFVRSFDGFSSAQKNQEQLLTLASILREDGKVFDEKVYYTAGYNSPVKLLNRNNEVWLIQKNEPTKENE |
| 预测分子量 | 38.7 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HEBP2重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**: "Recombinant HEBP2 exhibits heme-binding ability and modulates cellular oxidative stress"
**作者**: Smith A, et al.
**摘要**: 该研究通过原核表达系统成功纯化HEBP2重组蛋白，证实其与血红素结合的能力，并发现其在体外可降低H2O2诱导的氧化应激，提示HEBP2可能参与细胞抗氧化机制。
2. **文献名称**: "Structural characterization of human HEBP2 and its role in mitochondrial function"
**作者**: Chen L, et al.
**摘要**: 通过X射线晶体学解析HEBP2重组蛋白的三维结构，揭示其独特的α螺旋结构域可能介导线粒体膜相互作用，并发现HEBP2敲低导致线粒体呼吸链活性受损。
3. **文献名称**: "HEBP2 interacts with viral proteins and inhibits RNA virus replication"
**作者**: Wang Y, et al.
**摘要**: 研究利用重组HEBP2蛋白进行互作组学分析，发现其与多种RNA病毒蛋白结合，并通过体外实验证明HEBP2过表达显著抑制病毒复制，提示其抗病毒免疫潜能。
注：以上文献为示例，实际文献需通过PubMed或Google Scholar检索确认。近期研究(如2023年)可能涉及HEBP2在肿瘤代谢或神经退行性疾病中的调控机制。
**Background of HEBP2 Recombinant Protein**
HEBP2 (Heme-Binding Protein 2), also known as p22HBP or SOUL, is a conserved eukaryotic protein involved in cellular heme metabolism and homeostasis. It belongs to the HEBP protein family, which includes HEBP1. sharing structural similarities but differing in tissue distribution and regulatory roles. HEBP2 is ubiquitously expressed, with higher levels observed in tissues such as the liver, kidney, and brain. The protein binds heme, a critical iron-containing molecule essential for oxygen transport, energy production, and enzymatic reactions, suggesting its role in modulating heme availability or detoxification.
Structurally, HEBP2 adopts a β-barrel fold with a hydrophobic pocket for heme interaction. Studies indicate its involvement in intracellular heme trafficking, antioxidant defense, and protection against heme-induced oxidative stress. Dysregulation of HEBP2 has been linked to pathological conditions, including neurodegenerative disorders (e.g., Alzheimer’s disease) and cancers, where altered heme metabolism contributes to disease progression.
Recombinant HEBP2 is produced using expression systems like *E. coli* or mammalian cells, enabling large-scale purification for functional studies. Tagged versions (e.g., His-tag) facilitate isolation via affinity chromatography. Researchers utilize the recombinant protein to investigate heme-binding mechanisms, cellular signaling pathways, and therapeutic applications, such as targeting heme-related pathologies or developing diagnostic tools. Its role in modulating oxidative stress and apoptosis also makes it a candidate for studying cytoprotective strategies.
In summary, HEBP2 recombinant protein serves as a vital tool for unraveling heme biology and exploring therapeutic interventions in heme-associated diseases.
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