| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Hba |
| Uniprot No | P01942 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-142aa |
| 氨基酸序列 | VLSGEDKSNIKAAWGKIGGHGAEYGAEALERMFASFPTTKTYFPHFDVSHGSAQVKGHGKKVADALASAAGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLASHHPADFTPAVHASLDKFLASVSTVLTSKYR |
| 预测分子量 | 33.1 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3-4条与 **Hba(Hemoglobin subunit alpha)重组蛋白**相关的参考文献及其摘要概述：
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1. **文献名称**: *"Cloning and Expression of Recombinant Hba Protein in Escherichia coli"*
**作者**: Smith J, et al.
**摘要**: 该研究成功克隆了血红蛋白α亚基(Hba)基因，并利用大肠杆菌表达系统高效表达重组Hba蛋白。通过纯化和Western blot验证，证明重组蛋白具有天然Hba的抗原性，为后续免疫研究奠定基础。
2. **文献名称**: *"Hba Recombinant Protein as a Vaccine Candidate Against Bacterial Infection"*
**作者**: Wang L, et al.
**摘要**: 研究评估了重组Hba蛋白作为疫苗的潜力。在小鼠模型中，接种重组Hba可诱导强烈的Th1免疫反应，显著降低病原体载量，提示其在抗细菌感染中的潜在应用价值。
3. **文献名称**: *"Structural and Functional Analysis of Recombinant Hba in Oxygen Transport"*
**作者**: Kumar R, et al.
**摘要**: 通过X射线晶体学解析了重组Hba的三维结构，揭示了其与血红素结合的分子机制。功能实验表明，重组Hba在体外能有效结合氧气，为开发人工氧载体提供理论依据。
4. **文献名称**: *"Hba Recombinant Protein as a Diagnostic Marker for Anemia"*
**作者**: Zhang Y, et al.
**摘要**: 研究开发了一种基于重组Hba蛋白的ELISA检测方法，用于定量分析血清中游离Hba水平。临床样本验证显示，该方法对贫血患者的早期诊断具有高灵敏度和特异性。
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注：以上文献为示例，实际引用需根据具体研究领域(如细菌Hba或血红蛋白α亚基)查询真实数据库(如PubMed、ScienceDirect)。
Hemoglobin subunit alpha (HBA) recombinant protein is a genetically engineered form of the α-globin subunit, a critical component of hemoglobin, the oxygen-carrying molecule in red blood cells. Native hemoglobin is a tetramer composed of two α- and two β-globin subunits, each associated with a heme group that binds oxygen. HBA plays an essential role in maintaining hemoglobin's quaternary structure and oxygen-binding capacity.
The production of recombinant HBA emerged to address challenges in studying hemoglobinopathies (e.g., α-thalassemia), developing blood substitutes, and creating therapeutic interventions. Traditional methods of isolating hemoglobin from human blood posed risks of pathogen contamination, limited scalability, and ethical concerns. Recombinant DNA technology enabled the synthesis of HBA in heterologous systems like *E. coli*, yeast, or mammalian cells. These systems allow precise control over protein expression, post-translational modifications, and purity.
HBA recombinant protein has become a vital tool in biomedical research. It facilitates structural studies to understand mutations causing hemoglobin disorders and screens potential drugs targeting hemoglobin dysfunction. In therapeutics, recombinant HBA is explored for artificial oxygen carriers to mitigate blood shortages and transfusion risks. Additionally, it supports gene therapy research for hemoglobinopathies by serving as a reference for correcting genetic defects.
Despite advancements, challenges persist, such as achieving proper protein folding and heme incorporation *in vitro*. Recent progress in expression vector optimization, fusion tags, and cell-free systems has improved yields and functionality. Ongoing studies also focus on engineering HBA variants with enhanced stability or oxygen affinity for tailored medical applications.
Overall, HBA recombinant protein exemplifies the intersection of molecular biology and clinical innovation, offering scalable, safe solutions for both research and translational medicine.
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