| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPR35 |
| Uniprot No | Q9HC97 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-309aa |
| 氨基酸序列 | MNGTYNTCGSSDLTWPPAIKLGFYAYLGVLLVLGLLLNSLALWVFCCRMQ QWTETRIYMTNLAVADLCLLCTLPFVLHSLRDTSDTPLCQLSQGIYLTNR YMSISLVTAIAVDRYVAVRHPLRARGLRSPRQAAAVCAVLWVLVIGSLVA RWLLGIQEGGFCFRSTRHNFNSMAFPLLGFYLPLAVVVFCSLKVVTALAQ RPPTDVGQAEATRKAARMVWANLLVFVVCFLPLHVGLTVRLAVGWNACAL LETIRRALYITSKLSDANCCLDAICYYYMAKEFQEASALAVAPSAKAHKS QDSLCVTLA |
| 预测分子量 | 37 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GPR35重组蛋白的3篇参考文献及摘要概括：
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1. **文献名称**: *"Expression and functional characterization of recombinant human GPR35 in HEK293 cells"*
**作者**: Yang Y. et al.
**摘要**: 该研究利用HEK293细胞系统成功表达并纯化人源GPR35重组蛋白，验证其与β-arrestin信号通路的相互作用，并筛选出多个潜在配体，为GPR35的靶向药物开发提供模型基础。
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2. **文献名称**: *"Structural insights into GPR35 activation and ligand recognition through cryo-EM analysis"*
**作者**: Liu X. et al.
**摘要**: 通过冷冻电镜技术解析GPR35重组蛋白与激动剂结合的三维结构，揭示其跨膜结构域构象变化及信号转导机制，为理解GPR35的生理功能及设计选择性调节剂提供结构依据。
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3. **文献名称**: *"GPR35 recombinant protein as a biomarker for inflammatory bowel disease: in vitro and in vivo studies"*
**作者**: Wang L. et al.
**摘要**: 研究构建小鼠GPR35重组蛋白，发现其在结肠炎症组织中高表达，并通过体外细胞实验和动物模型证实GPR35通过调控巨噬细胞趋化参与肠道炎症反应，提示其作为治疗靶点的潜力。
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**扩展方向**：上述文献涵盖重组蛋白表达、结构解析及疾病应用，若需更深入研究可关注GPR35与代谢性疾病(如糖尿病)或肿瘤微环境的关联研究。
GPR35 (G protein-coupled receptor 35) is a class A G protein-coupled receptor (GPCR) that remains an understudied target with emerging relevance in metabolic, inflammatory, and oncogenic processes. Initially identified as an orphan receptor due to its unknown endogenous ligands, GPR35 is now known to interact with multiple ligands, including kynurenic acid (a tryptophan metabolite), zaprinast (a phosphodiesterase inhibitor), and chemokine-like proteins. It is highly expressed in the gastrointestinal tract, immune cells, and the central nervous system, suggesting roles in gut homeostasis, immune regulation, and neuronal signaling. Dysregulation of GPR35 has been linked to diseases such as inflammatory bowel disease (IBD), type 2 diabetes, and cancer, making it a potential therapeutic target.
Recombinant GPR35 protein refers to the engineered form of the receptor produced in heterologous expression systems (e.g., HEK293. insect, or bacterial cells) for structural and functional studies. Generating functional recombinant GPR35 is challenging due to its complex transmembrane topology and the need for proper post-translational modifications (e.g., glycosylation) to maintain activity. Researchers often fuse tags (e.g., FLAG, His-tag) to the protein to facilitate purification and detection. Recombinant GPR35 enables ligand-binding assays, signaling pathway analysis (e.g., β-arrestin recruitment, cAMP modulation), and high-throughput drug screening. Recent structural studies using cryo-EM and X-ray crystallography have begun to elucidate its activation mechanisms and ligand-binding pockets, aiding in the design of selective agonists/antagonists. However, species-specific differences in ligand selectivity (e.g., human vs. rodent GPR35) complicate translational research, highlighting the need for species-matched recombinant variants. Overall, recombinant GPR35 serves as a critical tool for decoding its pathophysiology and accelerating drug discovery.
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