| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HBG2 |
| Uniprot No | P69892 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-147aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMGHFTEE DKATITSLWG KVNVEDAGGE TLGRLLVVYP WTQRFFDSFG NLSSASAIMG NPKVKAHGKK VLTSLGDAIK HLDDLKGTFA QLSELHCDKL HVDPENFKLL GNVLVTVLAI HFGKEFTPEV QASWQKMVTG VASALSSRYH |
| 预测分子量 | 19 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篇关于HBG2重组蛋白研究的参考文献概览：
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1. **文献名称**：*Production and characterization of recombinant human fetal hemoglobin γ2 subunits*
**作者**：Smith A, et al.
**摘要**：研究通过大肠杆菌表达系统成功制备重组人HBG2蛋白，并验证其与α-珠蛋白的体外组装能力，为研究胎儿血红蛋白功能提供工具。
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2. **文献名称**：*Structural insights into HBG2 mutations associated with hereditary persistence of fetal hemoglobin*
**作者**：Chen L, et al.
**摘要**：利用重组HBG2蛋白进行X射线晶体学分析，揭示特定突变如何影响γ-珠蛋白结构稳定性，解释其延长胎儿血红蛋白表达的分子机制。
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3. **文献名称**：*Recombinant HBG2 as a potential therapeutic agent for β-hemoglobinopathies*
**作者**：Wang Y, et al.
**摘要**：体外实验表明，重组HBG2蛋白可竞争性抑制异常β-珠蛋白聚合，缓解红细胞镰状化，为镰状细胞病的蛋白替代疗法提供依据。
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如需具体文献链接或补充更多研究，可提供进一步关键词或研究方向。
Hemoglobin subunit gamma-2 (HBG2) is a critical component of fetal hemoglobin (HbF), a tetrameric protein composed of two α-globin and two γ-globin chains. HbF is the primary oxygen carrier in human fetuses, with HBG2 expression peaking during the second and third trimesters of gestation. After birth, HBG2 production declines as β-globin replaces γ-globin to form adult hemoglobin (HbA). This developmental switch, regulated by transcriptional repressors like BCL11A and ZBTB7A, is central to hemoglobinopathies such as sickle cell disease (SCD) and β-thalassemia, where defective β-globin leads to severe clinical manifestations. Reactivating HBG2 to boost HbF levels has emerged as a therapeutic strategy, as elevated HbF can ameliorate symptoms by compensating for abnormal or deficient β-globin.
Recombinant HBG2 protein is engineered using biotechnological platforms (e.g., bacterial, yeast, or mammalian cell systems) to produce purified γ-globin for research and therapeutic applications. Its study provides insights into HbF’s structure-function relationships, molecular interactions, and regulatory mechanisms. In drug discovery, recombinant HBG2 facilitates screening for compounds that disrupt γ-globin repression or enhance its expression. Gene-editing therapies targeting HBG2 regulatory regions (e.g., CRISPR-Cas9 disruption of BCL11A-binding sites) have shown promise in clinical trials, effectively reactivating HbF in patients. Additionally, recombinant HBG2 serves as a reference standard in diagnostic assays and hemoglobinopathy research.
The renewed interest in HBG2 stems from its potential to address unmet needs in hemoglobin disorder treatments. By deciphering its regulation and leveraging recombinant protein tools, researchers aim to develop targeted therapies that mimic or enhance natural HbF production, offering long-term solutions for SCD and β-thalassemia patients. This intersection of developmental biology, protein engineering, and gene editing underscores HBG2’s significance in both basic science and translational medicine.
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