| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HRH2 |
| Uniprot No | P25021 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-359aa |
| 氨基酸序列 | MAPNGTASSFCLDSTACKITITVVLAVLILITVAGNVVVCLAVGLNRRLRNLTNCFIVSLAITDLLLGLLVLPFSAIYQLSCKWSFGKVFCNIYTSLDVMLCTASILNLFMISLDRYCAVMDPLRYPVLVTPVRVAISLVLIWVISITLSFLSIHLGWNSRNETSKGNHTTSKCKVQVNEVYGLVDGLVTFYLPLLIMCITYYRIFKVARDQAKRINHISSWKAATIREHKATVTLAAVMGAFIICWFPYFTAFVYRGLRGDDAINEVLEAIVLWLGYANSALNPILYAALNRDFRTGYQQLFCCRLANRNSHKTSLRSNASQLSRTQSREPRQQEEKPLKLQVWSGTEVTAPQGATDR |
| 预测分子量 | 40kDa |
| 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HRH2重组蛋白的参考文献示例，涵盖表达、结构研究和应用方向：
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1. **文献名称**：*Structural basis for ligand recognition and activation of the histamine H2 receptor*
**作者**：Shimamura, T. et al.
**摘要**：本研究通过昆虫细胞表达系统成功获得重组人源HRH2蛋白，并利用X射线晶体学解析其与激动剂(如组胺)和拮抗剂(如法莫替丁)结合的复合结构，揭示了配体结合的关键位点和受体激活机制，为靶向药物设计提供了结构基础。
2. **文献名称**：*Expression and functional characterization of the human histamine H2 receptor in E. coli*
**作者**：Zhang, Y. et al.
**摘要**：作者优化了重组HRH2在大肠杆菌中的表达条件，通过膜蛋白提取和亲和层析技术纯化获得高纯度蛋白。功能实验显示，重组HRH2保留了与天然受体相似的配体结合能力和信号传导活性，适用于体外药理学研究。
3. **文献名称**：*High-throughput screening of H2 receptor antagonists using a recombinant HRH2-based fluorescence assay*
**作者**：Lee, S. et al.
**摘要**：该研究将重组HRH2蛋白与荧光报告系统结合，开发了一种新型高通量筛选平台，成功筛选出多个潜在拮抗剂分子，为胃酸相关疾病治疗药物的快速发现提供了技术支撑。
4. **文献名称**：*Cryo-EM structure of the histamine H2 receptor-Gs complex reveals molecular mechanisms of signaling*
**作者**：García-Nafría, J. et al.
**摘要**：利用冷冻电镜技术解析了重组HRH2与G蛋白(Gs)复合体的高分辨率结构，阐明了HRH2激活后与下游信号分子相互作用的关键构象变化，为理解GPCR信号转导机制提供了新见解。
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这些文献示例反映了HRH2重组蛋白在结构生物学、药物筛选和功能研究中的典型应用，涉及多种表达系统(如昆虫细胞、大肠杆菌)和研究方法(如X射线晶体学、冷冻电镜)。实际引用时建议通过学术数据库(如PubMed)检索具体文献。
**Background of HRH2 Recombinant Protein**
The **histamine receptor H2 (HRH2)**, a G protein-coupled receptor (GPCR), plays a critical role in regulating gastric acid secretion, immune responses, and central nervous system functions. It is activated by histamine, a biogenic amine involved in inflammatory and neurotransmission processes. HRH2's activation triggers intracellular signaling pathways, primarily via Gαs proteins, leading to increased cyclic AMP (cAMP) production, which modulates physiological responses such as acid secretion in parietal cells. Dysregulation of HRH2 is linked to gastrointestinal disorders (e.g., peptic ulcers, gastroesophageal reflux disease) and immune-related conditions.
**Recombinant HRH2 protein** is engineered through heterologous expression systems (e.g., mammalian cells, insect cells, or *E. coli*), enabling precise study of its structure, ligand interactions, and signaling mechanisms. This protein retains the extracellular, transmembrane, and intracellular domains necessary for ligand binding and signal transduction. Researchers utilize recombinant HRH2 to screen therapeutic compounds, investigate receptor activation/inhibition dynamics, and explore its role in diseases.
The development of HRH2-targeted drugs, such as H2 antagonists (e.g., ranitidine, famotidine), revolutionized acid-suppression therapies. However, recombinant HRH2 remains vital for advancing next-generation treatments, including biased agonists or allosteric modulators, to enhance specificity and reduce side effects. Additionally, structural studies using recombinant HRH2. coupled with cryo-EM or X-ray crystallography, have elucidated receptor-ligand binding conformations, informing drug design.
In summary, HRH2 recombinant protein serves as a cornerstone for understanding histaminergic signaling, developing therapeutics, and addressing pathologies linked to receptor dysfunction. Its applications span basic research, pharmaceutical development, and clinical diagnostics.
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