| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HEBP1 |
| Uniprot No | Q9NRV9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-189aa |
| 氨基酸序列 | MLGMIKNSLFGSVETWPWQVLSKGDKEEVAYEERACEGGKFATVEVTDKPVDEALREAMPKVAKYAGGTNDKGIGMGMTVPISFAVFPNEDGSLQKKLKVWFRIPNQFQSDPPAPSDKSVKIEEREGITVYSMQFGGYAKEADYVAQATRLRAALEGTATYRGDIYFCTGYDPPMKPYGRRNEIWLLKT |
| 预测分子量 | 48.6 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HEBP1重组蛋白的3篇文献摘要概述：
1. **文献名称**: *"HEBP1 acts as a mediator of oxidative stress-induced cell death in cancer cells"*
**作者**: Smith A, et al.
**摘要**: 研究揭示了HEBP1重组蛋白在氧化应激中的作用，发现其通过结合血红素并调节线粒体功能，促进活性氧(ROS)积累，从而诱导癌细胞凋亡。实验利用重组HEBP1蛋白验证了其促凋亡机制。
2. **文献名称**: *"Structural characterization of human HEBP1 and its interaction with heme"*
**作者**: Chen L, et al.
**摘要**: 通过X射线晶体学解析了重组HEBP1蛋白的三维结构，发现其具有独特的疏水腔结构域，可直接结合血红素分子。研究为HEBP1在血红素代谢和神经退行性疾病中的功能提供了结构基础。
3. **文献名称**: *"Recombinant HEBP1 modulates inflammatory responses in macrophages via heme scavenging"*
**作者**: Kim J, et al.
**摘要**: 研究利用大肠杆菌表达的重组HEBP1蛋白，证明其通过螯合游离血红素抑制巨噬细胞中NF-κB信号通路，降低炎症因子TNF-α和IL-6的产生，提示其在炎症性疾病中的潜在治疗价值。
注：上述文献信息为模拟示例，实际文献需通过PubMed、Web of Science等数据库检索获取。
**Background of HEBP1 Recombinant Protein**
HEBP1 (Heme Binding Protein 1), also known as p22HBP, is a conserved eukaryotic protein implicated in cellular heme homeostasis and stress response. Initially identified through its interaction with heme, HEBP1 binds porphyrins and metalloporphyrins with high affinity, suggesting a role in regulating intracellular heme availability. Structurally, HEBP1 contains a unique α-helical fold with distinct N- and C-terminal domains connected by a flexible linker, enabling conformational flexibility during ligand binding.
HEBP1 is ubiquitously expressed, with higher levels observed in tissues with active heme metabolism, such as the liver, kidney, and brain. Functionally, it is linked to antioxidant defense, as heme excess can catalyze reactive oxygen species (ROS) generation. By sequestering free heme, HEBP1 mitigates oxidative damage and modulates heme trafficking between organelles or proteins. Studies also associate HEBP1 with pathological conditions, including neurodegenerative disorders (e.g., Alzheimer’s disease), anemia, and cancers, where dysregulated heme metabolism contributes to disease progression.
Recombinant HEBP1 is produced using expression systems like *E. coli* or mammalian cells, often tagged for purification and detection. Its recombinant form retains native ligand-binding properties, making it a valuable tool for *in vitro* studies exploring heme-related pathways, drug screening, or structural analyses. Recent research highlights its potential as a biomarker or therapeutic target, particularly in diseases involving oxidative stress or iron dysregulation. Despite progress, the precise molecular mechanisms of HEBP1 in heme signaling and its interplay with other heme-handling proteins remain under investigation, underscoring its biological and clinical relevance.
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