| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HBA1 |
| Uniprot No | P69905 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMVL SPADKTNVKA AWGKVGAHAG EYGAEALERM FLSFPTTKTY FPHFDLSHGS AQVKGHGKKV ADALTNAVAH VDDMPNALSA LSDLHAHKLR VDPVNFKLLS HCLLVTLAAH LPAEFTPAVH ASLDKFLASV STVLTSKYR |
| 预测分子量 | 20 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3条关于HBA1重组蛋白研究的模拟参考文献(内容基于常见研究主题概括，非真实文献)：
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1. **文献名称**: *"Recombinant Human Hemoglobin α (HBA1) Expression in E. coli for Oxygen Therapeutic Development"*
**作者**: Smith J. et al.
**摘要**: 研究利用大肠杆菌表达系统高效表达重组HBA1蛋白，优化纯化工艺，并验证其氧结合能力，为开发血红蛋白基人工携氧载体提供基础数据。
2. **文献名称**: *"Structural and Functional Analysis of HBA1 Mutants via Recombinant Protein Technology"*
**作者**: Chen L. & Wang Y.
**摘要**: 通过重组蛋白技术构建HBA1常见突变体(如地中海贫血相关突变)，解析突变对血红蛋白四聚体稳定性及氧亲和力的影响，揭示致病机制。
3. **文献名称**: *"HBA1 Fusion Proteins as Drug Delivery Carriers: A Biophysical Study"*
**作者**: Gupta R. et al.
**摘要**: 将HBA1与靶向肽段融合表达，表征其载药能力和靶向性，证明重组HBA1可作为肿瘤特异性药物递送系统的潜在载体。
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**备注**：以上为基于HBA1重组蛋白常见研究方向的模拟内容，实际文献需通过PubMed、Web of Science等数据库检索获取。若需真实文献，建议使用关键词如 **"recombinant HBA1 protein"** 或 **"hemoglobin alpha expression"** 进行查询。
Hemoglobin subunit alpha-1 (HBA1) is a critical component of hemoglobin, the oxygen-carrying protein in red blood cells. It forms a heterotetramer with two alpha and two beta globin chains, creating the functional hemoglobin molecule essential for oxygen transport in vertebrates. Mutations in the HBA1 gene are linked to alpha-thalassemia and other hemoglobinopathies, driving interest in recombinant HBA1 protein production for biomedical research and therapeutic development.
Recombinant HBA1 is typically produced using expression systems like *E. coli* or yeast, enabling large-scale synthesis without relying on human blood sources. The process involves cloning the HBA1 gene into expression vectors, followed by fermentation, protein purification (often via affinity chromatography), and structural validation. This approach ensures batch consistency, eliminates pathogen contamination risks, and supports genetic modifications for functional studies.
Applications of recombinant HBA1 span multiple fields. In therapeutics, it serves as a platform for hemoglobin-based oxygen carriers (HBOCs) under investigation as blood substitutes. Researchers use it to study hemoglobinopathies, oxygen-binding mechanisms, and gene regulation. Additionally, it acts as a reference material in diagnostic assays for hemoglobin disorders. Recent advances include engineering recombinant HBA1 with enhanced stability or oxygen affinity, highlighting its potential in personalized medicine and gene therapy strategies targeting hemoglobin synthesis defects. The development of recombinant HBA1 exemplifies how synthetic biology tools can address challenges in both fundamental research and clinical translation for hematological diseases.
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