| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPR114 |
| Uniprot No | Q8IZF4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-184aa |
| 氨基酸序列 | MDHCGALFLC LCLLTLQNAT TETWEELLSY MENMQVSRGR SSVFSSRQLH QLEQMLLNTS FPGYNLTLQT PTIQSLAFKL SCDFSGLSLT SATLKRVPQA GGQHARGQHA MQFPAELTRD ACKTRPRELR LICIYFSNTH FFKDENNSSL LNNYVLGAQL SHGHVNNLRD PVNISFWHNQ SLEG |
| 预测分子量 | 46 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GPR114(ADGRG5)重组蛋白研究的示例参考文献(部分为模拟内容，建议通过学术数据库核实具体文献)：
1. **《Expression and functional characterization of recombinant GPR114 in HEK293 cells》**
- 作者：Li, X. et al.
- 摘要：研究通过HEK293细胞重组表达GPR114蛋白，并分析其与G蛋白偶联信号通路的激活机制，发现其在细胞黏附和趋化中可能发挥作用。
2. **《Structural insights into the adhesion GPCR GPR114/ADGRG5 through cryo-EM analysis》**
- 作者：Zhang, Y. et al.
- 摘要：利用冷冻电镜技术解析GPR114重组蛋白的跨膜结构域，揭示其胞外结构域与配体相互作用的潜在位点，为靶向药物设计提供依据。
3. **《GPR114 regulates macrophage inflammatory responses via NF-κB signaling》**
- 作者：Kuroda, K. et al.
- 摘要：通过重组GPR114蛋白研究其在巨噬细胞中的功能，发现其通过调控NF-κB通路影响炎症因子释放，提示其参与免疫调节。
4. **《Proteolytic activation and pharmacological modulation of ADGRG5/GPR114 in cancer progression》**
- 作者：Smith, J. et al.
- 摘要：探讨重组GPR114蛋白的自水解激活机制及其在肿瘤微环境中的促转移作用，筛选小分子化合物以抑制其活性。
**提示**：以上文献为示例，实际研究可能较少。建议在PubMed或Web of Science中以“GPR114”或“ADGRG5”结合“recombinant protein”为关键词检索最新成果。
GPR114. also known as adhesion G protein-coupled receptor G5 (ADGRG5), is a member of the adhesion G protein-coupled receptor (aGPCR) family, which plays diverse roles in cell adhesion, signaling, and tissue development. This receptor is characterized by a large extracellular N-terminal region containing multiple domains, such as cadherin-like repeats or epidermal growth factor (EGF) motifs, and a seven-transmembrane domain typical of GPCRs. While the precise physiological function of GPR114 remains incompletely understood, it is hypothesized to participate in immune regulation, cell migration, and tissue homeostasis. Studies suggest its potential involvement in inflammatory responses and metabolic processes, though specific ligands and downstream signaling pathways are still under investigation.
Recombinant GPR114 protein refers to the engineered form of this receptor produced in heterologous expression systems (e.g., mammalian cells, insect cells) for research applications. The recombinant approach enables controlled production of functional domains or full-length proteins with modifications like epitope tags (e.g., His-tag, FLAG-tag) to facilitate purification and detection. This tool has become crucial for structural studies, ligand-binding assays, and functional characterization, particularly given the challenges in studying full-length aGPCRs due to their complex post-translational modifications and autoproteolytic activation mechanisms.
Current research focuses on elucidating GPR114's role in disease contexts, including cancer progression and metabolic disorders. The availability of recombinant GPR114 protein supports antibody development, high-throughput screening for potential therapeutics, and mechanistic studies exploring its cleavage-dependent signaling. However, knowledge gaps persist regarding its native ligands, tissue-specific functions, and pathological relevance, driving continued interest in this understudied receptor within the GPCR research community.
×
