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Recombinant Human HBG1 protein

  • 中文名: 血红蛋白γ1(HBG1)重组蛋白
  • 别    名: HBG1;Hemoglobin subunit gamma-1
货号: PA1000-1404
Price: ¥询价
数量:
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产品详情

纯度>85%SDS-PAGE.
种属Human
靶点HBG1
Uniprot NoP69891
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间2-147aa
氨基酸序列GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTAVASALSSRYH
预测分子量23.0 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.

参考文献

以下是关于HBG1重组蛋白的模拟参考文献示例(仅供学术写作参考,具体文献需通过数据库查询):

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1. **标题**:*Expression and Purification of Recombinant HBG1 in E. coli for Functional Studies*

**作者**:Zhang L, et al.

**摘要**:本研究报道了在大肠杆菌中高效表达和纯化HBG1重组蛋白的方法,通过优化密码子和诱导条件提高产量,并验证其结构与天然蛋白的一致性。

2. **标题**:*Structural Analysis of HBG1 Reveals Key Residues for Oxygen Binding*

**作者**:Smith J, et al.

**摘要**:利用X射线晶体学解析HBG1重组蛋白的三维结构,发现特定氨基酸残基对其氧结合能力的关键作用,为血红蛋白功能进化提供依据。

3. **标题**:*HBG1 Recombinant Protein Ameliorates Symptoms in a Sickle Cell Disease Model*

**作者**:Chen H, et al.

**摘要**:在小鼠模型中,外源性HBG1重组蛋白通过竞争性抑制异常血红蛋白聚合,显著减轻镰状细胞贫血病理表型。

4. **标题**:*Comparative Study of HBG1 Expression Systems: Yeast vs. Mammalian Cells*

**作者**:Kumar R, et al.

**摘要**:对比酵母和哺乳动物细胞表达系统生产的HBG1重组蛋白,发现哺乳动物系统更利于维持蛋白翻译后修饰及功能完整性。

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建议通过PubMed、Google Scholar等平台检索真实文献,关键词如“HBG1 recombinant protein”“hemoglobin gamma-1 expression”。

背景信息

Hemoglobin subunit gamma-1 (HBG1) is a key 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, replacing embryonic hemoglobin by the 8th week of gestation and persisting until birth, after which it is gradually replaced by adult hemoglobin (HbA, α2β2). The HBG1 gene, located on chromosome 11 within the β-globin gene cluster, encodes the γ-globin chain, which differs from β-globin by 39 amino acids. These differences confer HbF with a higher oxygen affinity, facilitating efficient oxygen transfer across the placenta.

Recombinant HBG1 protein is produced using biotechnological platforms (e.g., bacterial, yeast, or mammalian expression systems) to enable studies of γ-globin structure-function relationships, hemoglobin switching mechanisms, and therapeutic applications. Research on HBG1 has gained momentum due to its clinical relevance in hemoglobinopathies like sickle cell disease and β-thalassemia. Reactivating HBG1 expression in adults can ameliorate symptoms by increasing HbF levels, a therapeutic strategy supported by genetic evidence (e.g., hereditary persistence of HbF). Recombinant HBG1 serves as a tool for drug screening, antibody development, and CRISPR-based gene editing studies aimed at reversing γ-globin silencing.

Recent advances include structural analyses of HbF using recombinant HBG1 to map oxygen-binding domains and investigate allosteric regulation. Additionally, recombinant proteins aid in exploring post-translational modifications and interactions with transcriptional regulators (e.g., BCL11A). These efforts aim to develop targeted therapies to induce HbF production, offering potential cures for debilitating blood disorders.

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