纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | HPX |
Uniprot No | P02790 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 24-462aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSTPLPPTSAHGNVAEGETKPDPDVTERC SDGWSFDATTLDDNGTMLFFKGEFVWKSHKWDRELISERWKNFPSPVDAA FRQGHNSVFLIKGDKVWVYPPEKKEKGYPKLLQDEFPGIPSPLDAAVECH RGECQAEGVLFFQGDREWFWDLATGTMKERSWPAVGNCSSALRWLGRYYC FQGNQFLRFDPVRGEVPPRYPRDVRDYFMPCPGRGHGHRNGTGHGNSTHH GPEYMRCSPHLVLSALTSDNHGATYAFSGTHYWRLDTSRDGWHSWPIAHQ WPQGPSAVDAAFSWEEKLYLVQGTQVYVFLTKGGYTLVSGYPKRLEKEVG TPHGIILDSVDAAFICPGSSRLHIMAGRRLWWLDLKSGAQATWTELPWPH EKVDGALCMEKSLGPNSCSANGPGLYLIHGPNLYCYSDVEKLNAAKALPQ PQNVTSLLGCTH |
预测分子量 | 52 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. |
以下为示例性参考文献(请注意,以下内容为模拟生成,建议通过学术数据库查询真实文献):
1. **"Recombinant Human Hemopexin (HPX) Production and Therapeutic Potential in Hemolytic Diseases"**
- 作者:Smith J, et al.
- 摘要:研究通过哺乳动物细胞表达系统高效生产重组HPX蛋白,验证其在体外和动物模型中缓解溶血释放的血红素毒性,为治疗镰状细胞病提供新策略。
2. **"Structural Characterization of Recombinant HPX and Its Interaction with Heme"**
- 作者:Li X, Wang Y.
- 摘要:通过X射线晶体学解析重组HPX的分子结构,揭示其血红素结合域的关键氨基酸位点,为设计靶向HPX的药物提供结构基础。
3. **"HPX Recombinant Protein Attenuates Sepsis-Induced Organ Damage via Heme Scavenging"**
- 作者:Garcia R, et al.
- 摘要:在小鼠脓毒症模型中,重组HPX通过清除游离血红素减少氧化应激和炎症反应,显著降低肝、肾损伤,提示其临床转化潜力。
4. **"Optimization of HPX Expression in E. coli for Large-Scale Biomedical Applications"**
- 作者:Chen L, et al.
- 摘要:优化大肠杆菌表达系统提高重组HPX产量,通过纯化工艺改进获得高活性蛋白,为工业级生产奠定技术基础。
**建议**:实际文献可通过PubMed、Web of Science等平台,以关键词"recombinant hemopexin"或"HPX protein engineering"检索近5年研究。
**Background of Recombinant HPX Protein**
Hemopexin (HPX) is a plasma glycoprotein primarily synthesized in the liver, renowned for its high-affinity binding to heme, a toxic byproduct of hemoglobin degradation. As the body’s primary heme-scavenging protein, HPX plays a critical role in mitigating oxidative stress and cellular damage caused by free heme, particularly during conditions like hemolysis, ischemia-reperfusion injury, or inflammation. By sequestering heme and delivering it to hepatocytes via receptor-mediated endocytosis, HPX facilitates heme iron recycling while preventing heme-induced lipid peroxidation and pro-inflammatory responses.
Recombinant HPX (rHPX) is engineered using biotechnological approaches, often expressed in mammalian cell systems (e.g., CHO cells) or yeast to ensure proper post-translational modifications, such as glycosylation, which is essential for its stability and function. The production of rHPX addresses limitations in isolating the native protein from plasma, such as low yield and ethical concerns. Recent advances in protein engineering have further optimized its heme-binding capacity and pharmacokinetic properties.
Research highlights rHPX’s therapeutic potential in hemolytic disorders (e.g., sickle cell disease), neurodegenerative diseases (e.g., Alzheimer’s), and sepsis, where heme toxicity exacerbates pathology. Preclinical studies demonstrate its efficacy in reducing oxidative damage and inflammation. However, challenges remain in scaling production, ensuring cost-effectiveness, and validating long-term safety. Ongoing efforts focus on enhancing delivery systems and exploring synergistic therapies with other heme-targeting agents.
In summary, recombinant HPX represents a promising biologic to counteract heme-driven pathologies, bridging gaps in current treatments by targeting the root cause of heme toxicity. Its development underscores the intersection of biochemistry, biotechnology, and translational medicine.
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