| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPRC5A |
| Uniprot No | Q8NFJ5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 269-357aa |
| 氨基酸序列 | TKQRNPMDYPVEDAFCKPQLVKKSYGVENRAYSQEEITQGFEETGDTLYAPYSTHFQLQNQPPQKEFSIPRAHAWPSPYKDYEVKKEGS |
| 预测分子量 | 37.0 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. |
以下是3-4篇关于GPRC5A重组蛋白的虚构参考文献示例(基于研究领域常见方向，非真实文献)：
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1. **文献名称**：*Structural Insights into GPRC5A Activation Mechanism Using Recombinant Protein Expression*
**作者**：Li, X. et al.
**摘要**：本研究通过大肠杆菌系统表达并纯化GPRC5A重组蛋白，解析其晶体结构，揭示了该受体胞外域的配体结合模式及跨膜区的构象变化，为靶向GPRC5A的药物设计提供结构基础。
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2. **文献名称**：*GPRC5A Recombinant Protein Suppresses Lung Cancer Progression via EGFR Signaling Modulation*
**作者**：Wang, Y. et al.
**摘要**：利用哺乳动物细胞系表达的重组GPRC5A蛋白，研究发现其可通过抑制EGFR磷酸化阻断非小细胞肺癌细胞的增殖和迁移，提示其作为肿瘤治疗靶点的潜力。
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3. **文献名称**：*Recombinant GPRC5A Regulates Inflammatory Response in Macrophages through TLR4 Interaction*
**作者**：Müller, R. et al.
**摘要**：通过真核表达系统制备功能性GPRC5A重组蛋白，证明其通过直接结合TLR4抑制NF-κB通路活化，缓解脂多糖诱导的巨噬细胞炎症反应，为免疫调节研究提供新思路。
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4. **文献名称**：*Development of a High-Yield GPRC5A Recombinant Protein Production Platform for Drug Screening*
**作者**：Chen, H. et al.
**摘要**：优化昆虫细胞-杆状病毒系统的重组GPRC5A蛋白表达条件，实现毫克级可溶性蛋白制备，并建立基于表面等离子体共振(SPR)的配体筛选模型，加速靶向该受体的药物发现。
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注：以上文献信息为虚构，仅用于示例参考。实际研究中请通过PubMed或Web of Science检索真实文献。
GPRC5A (G Protein-Coupled Receptor Class C Group 5 Member A) is an orphan receptor belonging to the G protein-coupled receptor (GPCR) family, characterized by its seven transmembrane domains and extracellular ligand-binding regions. Initially identified as a retinoic acid-inducible gene, it is predominantly expressed in lung tissue and plays ambiguous roles in cellular processes, including proliferation, differentiation, and apoptosis. Its dual regulatory functions in cancer—acting as both a tumor suppressor and promoter—have sparked significant research interest, particularly in lung, pancreatic, and colorectal cancers.
Structurally, recombinant GPRC5A proteins are engineered to retain functional domains, such as the extracellular N-terminal region critical for ligand interaction and intracellular loops involved in G protein signaling. These proteins are typically produced in mammalian expression systems (e.g., HEK293 cells) or bacterial systems, with purification tags (e.g., His-tag) for experimental applications. Recombinant forms enable studies on receptor oligomerization, post-translational modifications (e.g., glycosylation), and interactions with signaling partners like EGFR or Hedgehog pathway components.
Research highlights GPRC5A's involvement in maintaining epithelial cell integrity and modulating inflammatory responses. Its downregulation in lung adenocarcinoma correlates with poor prognosis, while overexpression in some contexts promotes metastasis. Recombinant GPRC5A tools are vital for deciphering its paradoxical roles, screening therapeutic ligands, and exploring its potential as a biomarker or drug target. Ongoing studies aim to resolve its endogenous ligands and precise mechanistic contributions to disease pathways.
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