| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AHSP |
| 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 | MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN YYRQQVTGEP QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP SS |
| 预测分子量 | 38.8kDa |
| 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3篇关于AHSP重组蛋白的文献摘要概览：
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1. **文献名称**: "Role of Alpha-Hemoglobin Stabilizing Protein in Normal Erythropoiesis and β-Thalassemia"
**作者**: Yu et al.
**摘要**: 研究揭示了AHSP通过结合游离的α-血红蛋白单体，防止其聚集并促进红细胞成熟。通过重组AHSP蛋白实验，证实其在β-地中海贫血患者中可改善无效红系造血，为潜在治疗策略提供依据。
2. **文献名称**: "Structural Basis for AHSP-mediated Stabilization of α-Hemoglobin"
**作者**: Gell et al.
**摘要**: 利用重组AHSP蛋白的晶体结构分析，阐明了AHSP与α-血红蛋白结合的分子机制。研究发现AHSP通过特定的疏水界面和氢键网络稳定α-血红蛋白的构象，防止氧化损伤。
3. **文献名称**: "Recombinant AHSP Production in E. coli and Functional Characterization"
**作者**: Santos et al.
**摘要**: 报道了一种高效的大肠杆菌表达系统用于重组AHSP蛋白的制备，并通过体外实验验证其与α-血红蛋白的结合活性。该方法为大规模生产研究级AHSP提供了技术基础。
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注：以上文献为示例性概括，实际文献需通过PubMed或Web of Science等平台检索。如需具体论文，建议结合关键词“AHSP recombinant protein”“Alpha-Hemoglobin Stabilizing Protein”进一步筛选。
**Background of AHSP Recombinant Protein**
Alpha-hemoglobin-stabilizing protein (AHSP), also known as erythroid-associated factor, is a molecular chaperone critical for hemoglobin homeostasis in red blood cells. Discovered in the early 2000s, AHSP specifically binds to free α-hemoglobin subunits, preventing their aggregation, oxidative damage, and precipitation during erythropoiesis. This stabilization is vital because α- and β-hemoglobin subunits must be synthesized in precise stoichiometric ratios to form functional hemoglobin tetramers. Imbalances, such as excess α-hemoglobin in β-thalassemia, lead to toxic aggregates and hemolytic anemia. AHSP acts as a buffer, ensuring α-hemoglobin stability until β-subunits become available.
Structurally, AHSP shares homology with β-hemoglobin, enabling it to mimic β-subunits and form a stable complex with α-hemoglobin. This interaction shields reactive heme groups, reducing oxidative stress and cellular damage. Studies using AHSP knockout models highlight its physiological importance; deficient mice exhibit anemia, hemoglobin precipitation, and shortened red blood cell lifespan.
Recombinant AHSP protein is produced via bacterial (e.g., *E. coli*) or mammalian expression systems, followed by purification techniques like affinity chromatography. Its applications span *in vitro* studies of hemoglobin assembly, oxidative stress mechanisms, and genetic blood disorders. Additionally, recombinant AHSP serves as a tool to explore therapeutic strategies for thalassemias and hemoglobinopathies, where modulating AHSP expression could alleviate α-subunit toxicity. Recent research also investigates its potential in stabilizing hemoglobin-based oxygen carriers (HBOCs) for blood substitutes.
Overall, AHSP recombinant protein is a key reagent in hematology research, bridging molecular insights into hemoglobin biology and translational approaches for treating red blood cell disorders.
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