| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | Hbb-b2 |
| Uniprot No | P02089 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-147aa |
| 氨基酸序列 | VHLTDAEKSAVSCLWAKVNPDEVGGEALGRLLVVYPWTQRYFDSFGDLSSASAIMGNPKVKAHGKKVITAFNEGLKNLDNLKGTFASLSELHCDKLHVDPENFRLLGNAIVIVLGHHLGKDFTPAAQAAFQKVVAGVATALAHKYH |
| 预测分子量 | 17.7 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Hbb-b2重组蛋白的虚构参考文献示例(仅供信息参考，非真实文献)：
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1. **文献名称**: *Expression and Purification of Recombinant Hbb-b2 Protein in E. coli*
**作者**: Zhang L. et al.
**摘要**: 本研究报道了通过大肠杆菌表达系统高效表达Hbb-b2重组蛋白的优化方法，采用His标签纯化技术获得高纯度蛋白，并通过质谱验证其正确折叠，为后续功能研究奠定基础。
2. **文献名称**: *Structural Characterization of Hbb-b2 Recombinant Protein Using X-ray Crystallography*
**作者**: Patel R., Kim S.
**摘要**: 通过X射线晶体学解析Hbb-b2重组蛋白的三维结构，揭示了其与氧气结合的活性位点特征，为理解β-血红蛋白亚基在氧运输中的作用提供结构生物学依据。
3. **文献名称**: *Hbb-b2 Recombinant Protein Ameliorates Anemia in a Mouse Model of β-Thalassemia*
**作者**: Gupta A. et al.
**摘要**: 实验证明，外源性Hbb-b2重组蛋白可显著改善β-地中海贫血模型小鼠的红细胞形态和血红蛋白水平，提示其潜在治疗应用价值。
4. **文献名称**: *Functional Analysis of Hbb-b2 Mutants via Recombinant Protein Expression*
**作者**: Müller J. et al.
**摘要**: 通过构建Hbb-b2基因突变体的重组蛋白，评估不同突变对其与α-血红蛋白结合能力的影响，揭示了特定位点突变导致血红蛋白功能障碍的分子机制。
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**备注**：以上文献为示例性内容，实际文献需通过PubMed、Web of Science等学术平台检索关键词(如"Hbb-b2 recombinant protein"或"hemoglobin subunit beta-2")获取。
**Background of Hbb-b2 Recombinant Protein**
The Hbb-b2 (hemoglobin subunit beta-2) recombinant protein is a genetically engineered form of the β-globin chain, a critical component of hemoglobin responsible for oxygen transport in vertebrates. Hemoglobin, a tetrameric protein, typically consists of two α-globin and two β-globin chains. In mice, the Hbb-b2 gene encodes one of the β-globin isoforms expressed during fetal development, playing a key role in ensuring efficient oxygen delivery to developing tissues.
Recombinant Hbb-b2 is produced using expression systems such as *E. coli*, yeast, or mammalian cells, enabling large-scale purification for research and therapeutic applications. Its production often involves cloning the Hbb-b2 gene into expression vectors, followed by protein extraction, refolding (if necessary), and validation via techniques like SDS-PAGE or mass spectrometry.
This recombinant protein is widely used to study hemoglobinopathies, including β-thalassemia and sickle cell disease, which arise from mutations in β-globin genes. By analyzing Hbb-b2 structure-function relationships, researchers gain insights into hemoglobin assembly, stability, and oxygen-binding kinetics. Additionally, it serves as a tool for developing gene therapies, protein replacement strategies, or blood substitutes.
In recent years, Hbb-b2 has also been employed in evolutionary studies to understand globin gene regulation and species-specific adaptations. Its role in murine models, where Hbb-b2 mutations mimic human hemoglobin disorders, highlights its translational relevance. Overall, Hbb-b2 recombinant protein bridges basic research and clinical innovation, offering a versatile platform to address both mechanistic and therapeutic challenges in hematology.
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