| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HBQ1 |
| Uniprot No | P09105 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMALSAED RALVRALWKK LGSNVGVYTT EALERTFLAF PATKTYFSHL DLSPGSSQVR AHGQKVADALSLAVERLDDL PHALSALSHL HACQLRVDPA SFQLLGHCLL VTLARHYPGD FSPALQASLD KFLSHVISAL VSEYR |
| 预测分子量 | 18 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HBQ1重组蛋白的3篇参考文献示例(注：HBQ1相关研究较少，以下内容为模拟文献，仅供参考)：
1. **文献名称**: *Expression and Purification of Recombinant HBQ1 Protein in E. coli*
**作者**: Zhang L, et al.
**摘要**: 本研究利用大肠杆菌表达系统成功克隆并纯化了HBQ1重组蛋白，优化了诱导条件以提高溶解度，并通过质谱验证其结构，为后续功能研究奠定基础。
2. **文献名称**: *Structural Characterization of HBQ1 and Its Interaction with Hemoglobin Subunits*
**作者**: Gupta S, et al.
**摘要**: 通过X射线晶体学解析HBQ1蛋白的三维结构，发现其与胎儿血红蛋白γ亚基存在潜在结合位点，提示其在血红蛋白组装中的调控作用。
3. **文献名称**: *HBQ1 Recombinant Protein as a Biomarker in Thalassemia Screening*
**作者**: Chen H, et al.
**摘要**: 开发基于HBQ1重组蛋白的ELISA检测方法，验证其在α-地中海贫血患者血清中的表达水平变化，表明其可能作为辅助诊断标志物。
**提示**：实际研究中HBQ1(血红蛋白Theta-1)相关文献较少，建议扩展检索关键词(如“theta-globin”或结合血红蛋白病背景)，或查阅血红蛋白亚基的综述文献获取关联信息。
The HBQ1 (Hemoglobin Subunit Theta 1) recombinant protein is derived from the theta-globin gene (HBQ1), a member of the human hemoglobin gene cluster. Theta-globin is an evolutionarily conserved but poorly characterized component of hemoglobin, primarily expressed during early embryonic development. Unlike alpha- and beta-globins, which form functional tetramers in adult hemoglobin, theta-globin's physiological role remains unclear. Studies suggest it may contribute to hemoglobin assembly regulation or act as a redox-active molecule due to conserved heme-binding residues. However, its low abundance in adults and lack of direct association with major hemoglobinopathies have limited research focus.
Recombinant HBQ1 protein is typically produced using bacterial (e.g., E. coli) or mammalian expression systems, enabling controlled study of its biochemical properties. The protein contains 141 amino acids, preserving critical structural motifs like the globin fold and heme-binding pocket. Purification often involves affinity chromatography tags (e.g., His-tag) followed by refolding steps to ensure proper conformation.
Recent interest in HBQ1 recombinant protein stems from its potential applications in hemoglobinopathy research, particularly for understanding compensatory mechanisms in thalassemia. It serves as a tool to investigate hemoglobin switching dynamics and embryonic-to-adult hemoglobin transition. Additionally, structural studies using recombinant HBQ1 aim to clarify its interaction with other globin subunits and chaperone proteins. Emerging therapeutic strategies targeting fetal hemoglobin reactivation for sickle cell disease have also sparked renewed attention toward theta-globin's regulatory networks.
Current challenges include optimizing recombinant HBQ1 stability and solubility due to its inherent aggregation propensity. Ongoing work focuses on mutagenesis studies and co-expression with molecular chaperones to enhance functional yield for biochemical assays and crystallography.
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