| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GRPR |
| Uniprot No | P30550 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-384aa |
| 氨基酸序列 | MALNDCFLLNLEVDHFMHCNISSHSADLPVNDDWSHPGILYVIPAVYGVI ILIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLITCAPVDASR YLADRWLFGRIGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQA SHALMKICLKAAFIWIISMLLAIPEAVFSDLHPFHEESTNQTFISCAPYP HSNELHPKIHSMASFLVFYVIPLSIISVYYYFIAKNLIQSAYNLPVEGNI HVKKQIESRKRLAKTVLVFVGLFAFCWLPNHVIYLYRSYHYSEVDTSMLH FVTSICARLLAFTNSCVNPFALYLLSKSFRKQFNTQLLCCQPGLIIRSHS TGRSTTCMTSLKSTNPSVATFSLINGNICHERYV |
| 预测分子量 | 68 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GRPR(胃泌素释放肽受体)重组蛋白的参考文献示例(仅供参考，建议通过学术数据库核实具体文献)：
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1. **文献名称**：*Expression and Purification of Recombinant GRPR in Mammalian Cells for Ligand Binding Studies*
**作者**：Smith, J., et al.
**摘要**：该研究报道了在HEK293细胞中高效表达重组GRPR蛋白的方法，并通过亲和层析纯化获得功能性受体。研究验证了其与胃泌素释放肽(GRP)的特异性结合能力，为后续受体信号转导研究奠定基础。
2. **文献名称**：*Structural Characterization of GRPR Using Cryo-EM: Insights into G-Protein Coupling*
**作者**：Lee, H., & Zhang, Y.
**摘要**：利用冷冻电镜技术解析了重组GRPR与G蛋白复合体的三维结构，揭示了受体激活状态下的构象变化及关键结合域，为设计靶向GRPR的药物提供了结构生物学依据。
3. **文献名称**：*Targeted Imaging of GRPR-Expressing Tumors with Recombinant Protein-Based Probes*
**作者**：Wang, Q., et al.
**摘要**：开发了一种基于重组GRPR蛋白的荧光探针，可特异性识别肿瘤细胞表面过表达的GRPR，在体内外实验中实现了高对比度的肿瘤成像，具有潜在诊断应用价值。
4. **文献名称**：*Functional Analysis of GRPR Mutants in Cancer Cell Proliferation*
**作者**：Garcia-Rojas, M., et al.
**摘要**：通过构建GRPR重组蛋白的突变体，发现其磷酸化位点突变可抑制下游ERK信号通路，显著降低肿瘤细胞的增殖和迁移能力，提示GRPR作为癌症治疗靶点的潜力。
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**注意**：以上文献信息为示例，实际文献需通过PubMed、Web of Science等平台检索。如需具体文章，可提供更详细的研究方向或年份要求。
**Background of GRPR Recombinant Protein**
The gastrin-releasing peptide receptor (GRPR), a member of the G protein-coupled receptor (GPCR) family, binds to its endogenous ligand, gastrin-releasing peptide (GRP), to regulate diverse physiological processes. Structurally, GRPR contains seven transmembrane domains and signals primarily through Gq/11 proteins, activating phospholipase C (PLC), intracellular calcium mobilization, and protein kinase C (PKC) pathways. It plays roles in digestion, smooth muscle contraction, and neurotransmitter release, while aberrant GRPR signaling is implicated in cancer progression, inflammation, and neurological disorders.
GRPR overexpression is observed in cancers like prostate, breast, and lung, where it promotes cell proliferation, survival, and metastasis. This makes GRPR a therapeutic and diagnostic target. Recombinant GRPR proteins, engineered via genetic cloning and expression in host systems (e.g., *E. coli*, mammalian cells), retain functional receptor domains for *in vitro* studies. These proteins enable ligand-binding assays, receptor signaling studies, and drug screening, particularly for GRPR antagonists or imaging agents.
The development of GRPR recombinant proteins supports cancer research, including targeted therapies (e.g., GRPR-linked toxins) and molecular imaging probes (e.g., radiolabeled GRP analogs). Challenges include maintaining receptor stability and post-translational modifications during production. Nonetheless, GRPR recombinant tools remain vital for elucidating its pathobiology and advancing precision medicine approaches.
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