| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERAF |
| Uniprot No | Q9NZD4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-102aa |
| 氨基酸序列 | MALLKANKDLISAGLKEFSVLLNQQVFNDPLVSEEDMVTVVEDWMNFYINYYRQQVTGEPQERDKALQELRQELNTLANPFLAKYRDFLKSHELPSHPPPSS |
| 分子量 | 38.8 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人ERAF蛋白的3篇代表性文献的简要信息(注：ERAF可能指与抗原处理相关的内质网氨基肽酶，此处模拟文献供参考)：
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1. **文献名称**：*Structural insights into ERAAP function in MHC-I antigen processing*
**作者**：Wang, C. et al.
**摘要**：该研究解析了重组人ERAF蛋白的晶体结构，揭示其氨基肽酶活性对MHC-I类分子抗原肽的修剪机制，为免疫应答调控提供结构基础。
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2. **文献名称**：*Recombinant human ERAF expression in E. coli and its enzymatic characterization*
**作者**：Zhang, Y. et al.
**摘要**：报道利用大肠杆菌系统高效表达重组人ERAF蛋白的方法，并通过质谱验证其剪切特定抗原前体肽的功能，证明其在体外抗原呈递中的关键作用。
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3. **文献名称**：*ERAF deficiency alters erythroid differentiation via modulating TGF-β signaling*
**作者**：Kumar, S. et al.
**摘要**：研究重组人ERAF蛋白在红细胞分化中的调控作用，发现其缺失通过TGF-β通路异常活化抑制红系祖细胞增殖，提示其在血液疾病中的潜在影响。
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**注**：ERAF常被称作ERAAP(ERAP1/2)，若需真实文献建议通过学术数据库检索确认。
Recombinant human Erythroid-Associated Factor (ERAF) protein, also known as α-hemoglobin-stabilizing protein (AHSP), plays a critical role in red blood cell development by regulating hemoglobin synthesis. Naturally produced during erythropoiesis, ERAF binds specifically to free α-globin subunits, acting as a molecular chaperone to prevent their aggregation and oxidative damage. This interaction ensures the balanced assembly of α- and β-globin chains into functional hemoglobin tetramers, crucial for oxygen transport.
Dysregulation of ERAF expression is linked to β-thalassemia and other hemoglobinopathies, where excess α-globin precipitates cause ineffective erythropoiesis and cellular damage. Recombinant ERAF, typically expressed in bacterial or mammalian systems, retains its ability to stabilize α-globin, making it a valuable tool for studying these disorders. Researchers use it to investigate disease mechanisms, screen therapeutic agents, and explore protein-folding dynamics. Its therapeutic potential includes strategies to mitigate globin imbalance in transfusion-dependent anemias or enhance ex vivo red blood cell production. Structural studies of recombinant ERAF have further elucidated its folding pathways and binding interfaces, offering insights for engineering targeted hemoglobin regulators. Overall, this protein bridges basic research and translational applications in hematology and genetic medicine.
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