| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Hepc |
| Uniprot No | P81172 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-84aa |
| 氨基酸序列 | SVFPQQTGQLAELQPQDRAGARASWMPMFQRRRRRDTHFPICIFCCGCCH RSKCGMCCKT |
| 预测分子量 | 32 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Hepcidin(Hepc)重组蛋白的3篇参考文献示例(注：部分信息为模拟概括，实际文献需通过学术数据库检索确认)：
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1. **《Expression and Functional Characterization of Recombinant Human Hepcidin in Saccharomyces cerevisiae》**
*作者：Smith A, et al.*
**摘要**：研究通过酵母表达系统成功制备重组人Hepcidin，并验证其抑制铁转运蛋白Ferroportin的能力，为大规模生产治疗铁代谢紊乱的Hepcidin提供新方法。
2. **《Recombinant Hepcidin Ameliorates Iron Overload in a Mouse Model of Hereditary Hemochromatosis》**
*作者：Chen L, et al.*
**摘要**：在小鼠遗传性血色素沉着症模型中，注射重组Hepcidin显著降低血清铁水平和肝脏铁沉积，证实其作为铁过载疗法的潜力。
3. **《Optimization of E. coli Expression System for High-Yield Production of Biologically Active Hepcidin-25》**
*作者：Kim H, et al.*
**摘要**：通过优化大肠杆菌表达条件(如诱导温度、融合标签)，实现高产量可溶性Hepcidin-25的纯化，并证明其体外抑制铁释放的活性。
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**备注**：实际研究中，Hepcidin重组蛋白的研究常聚焦于表达系统优化(如原核/真核系统)、体内外功能验证(铁代谢调控)及疾病治疗应用(如贫血、血色素沉着症)。建议通过PubMed或Web of Science检索关键词“recombinant hepcidin”获取具体文献。
Hepcidin, a key iron-regulatory hormone primarily synthesized in the liver, plays a central role in maintaining systemic iron homeostasis. Discovered in 2000. this small, cysteine-rich peptide regulates dietary iron absorption and macrophage iron recycling by binding to the iron exporter ferroportin, triggering its internalization and degradation. Dysregulation of hepcidin is implicated in various iron-related disorders, including hereditary hemochromatosis (low hepcidin) and anemia of chronic disease (elevated hepcidin).
Recombinant hepcidin (rhHepcidin) is produced via genetic engineering, typically using bacterial (E. coli) or mammalian expression systems. Its production addresses the challenges of natural hepcidin's short half-life and low abundance. RhHepcidin retains the bioactive 25-amino-acid form, including eight conserved cysteines forming four disulfide bonds critical for function. Structural authenticity is ensured through advanced purification and folding techniques.
Therapeutically, rhHepcidin shows promise for treating iron overload disorders by mimicking endogenous hepcidin activity. Conversely, hepcidin antagonists are explored for anemia management in chronic inflammation. Research also investigates its role in infections, as pathogens require iron for proliferation, and hepcidin-mediated iron sequestration constitutes a host defense mechanism. Challenges include optimizing pharmacokinetics and minimizing off-target effects. Recent advances in peptide engineering, such as PEGylation or fusion proteins, aim to enhance stability and efficacy.
As a research tool, rhHepcidin enables mechanistic studies of iron metabolism and drug screening. Its development underscores the intersection of molecular biology and clinical medicine, offering potential therapies for globally prevalent iron disorders.
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