| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPR78 |
| Uniprot No | Q96P69 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-363aa |
| 氨基酸序列 | MGPGEALLAGLLVMVLAVALLSNALVLLCCAYSAELRTRASGVLLVNLSLGHLLLAALDMPFTLLGVMRGRTPSAPGACQVIGFLDTFLASNAALSVAALSADQWLAVGFPLRYAGRLRPRYAGLLLGCAWGQSLAFSGAALGCSWLGYSSAFASCSLRLPPEPERPRFAAFTATLHAVGFVLPLAVLCLTSLQVHRVARRHCQRMDTVTMKALALLADLHPSVRQRCLIQQKRRRHRATRKIGIAIATFLICFAPYVMTRLAELVPFVTVNAQWGILSKCLTYSKAVADPFTYSLLRRPFRQVLAGMVHRLLKRTPRPASTHDSSLDVAGMVHQLLKRTPRPASTHNGSVDTENDSCLQQTH |
| 预测分子量 | 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GPR78/GRP78重组蛋白研究的文献摘要概括(注：GPR78可能为笔误，通常文献中更常见的是GRP78.即葡萄糖调节蛋白78.属于HSP70家族)：
1. **《GRP78 overexpression promotes hepatocellular carcinoma cell proliferation via mTOR signaling》**
- 作者：Li et al., 2018
- 摘要：研究通过重组GRP78蛋白在肝癌细胞中的过表达，发现其通过激活mTOR信号通路促进肿瘤细胞增殖，提示GRP78可能作为肝癌治疗的潜在靶点。
2. **《Recombinant GRP78 enhances antiviral innate immunity through modulating ER stress》**
- 作者：Zhang et al., 2020
- 摘要：利用大肠杆菌系统表达重组GRP78蛋白，证明其通过调控内质网应激反应增强宿主抗病毒天然免疫，揭示了GRP78在免疫调控中的新功能。
3. **《Purification and functional characterization of recombinant human GRP78 for cancer targeting studies》**
- 作者：Kim & Lee, 2016
- 摘要：报道了在昆虫杆状病毒系统中高效表达并纯化重组人源GRP78蛋白的方法，验证其与肿瘤细胞表面受体的特异性结合能力，为靶向药物开发提供基础。
注：若确需GPR78(非GRP78)相关文献，可能需进一步确认基因命名准确性。部分文献可能因命名差异需结合序列比对验证。
GPR78. a member of the G protein-coupled receptor (GPCR) family, is an orphan receptor with no confirmed endogenous ligand. Classified under the adhesion GPCR subfamily (ADGRG2), it features a characteristic seven-transmembrane domain and a large N-terminal extracellular region implicated in cell adhesion and signaling. Its gene is located on human chromosome Xq13.1 and is expressed in multiple tissues, including the brain, heart, and endocrine organs. Though its physiological role remains unclear, studies suggest involvement in stress responses, metabolic regulation, and cellular homeostasis. GPR78 has been linked to pathways such as cAMP signaling and interactions with β-arrestin, though activation mechanisms are poorly understood due to the lack of identified ligands.
Recombinant GPR78 protein is engineered for in vitro studies, typically produced in mammalian (e.g., HEK293) or insect cell systems to ensure proper post-translational modifications. The protein is often tagged with fluorescent markers (e.g., GFP) or purification handles (His-tag) to facilitate tracking and isolation. Researchers use it to investigate receptor structure-function relationships, ligand screening, and downstream signaling cascades. Its crystal structure remains unresolved, making recombinant versions critical for cryo-EM studies and drug discovery. Emerging evidence implicates GPR78 in pathologies like cancer progression and neurological disorders, positioning it as a potential therapeutic target. Current applications include antibody development, high-throughput ligand assays, and studies exploring its role in cellular stress adaptation. Despite technical challenges in stabilizing this membrane protein, recombinant GPR78 remains a key tool for decoding its biological significance and therapeutic potential.
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