| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GALR4 |
| Uniprot No | Q8TDV0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-419aa |
| 氨基酸序列 | MLAAAFADSNSSSMNVSFAHLHFAGGYLPSDSQDWRTIIPALLVAVCLVGFVGNLCVIGILLHNAWKGKPSMIHSLILNLSLADLSLLLFSAPIRATAYSKSVWDLGWFVCKSSDWFIHTCMAAKSLTIVVVAKVCFMYASDPAKQVSIHNYTIWSVLVAIWTVASLLPLPEWFFSTIRHHEGVEMCLVDVPAVAEEFMSMFGKLYPLLAFGLPLFFASFYFWRAYDQCKKRGTKTQNLRNQIRSKQVTVMLLSIAIISALLWLPEWVAWLWVWHLKAAGPAPPQGFIALSQVLMFSISSANPLIFLVMSEEFREGLKGVWKWMITKKPPTVSESQETPAGNSEGLPDKVPSPESPASIPEKEKPSSPSSGKGKTEKAEIPILPDVEQFWHERDTVPSVQDNDPIPWEHEDQETGEGVK |
| 预测分子量 | 46,6 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GALR4(甘丙肽受体4型)重组蛋白研究的假设性参考文献示例，供参考格式和内容方向。实际文献需通过学术数据库检索获取：
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1. **标题**：*Expression and Functional Characterization of Recombinant GALR4 in Mammalian Cells*
**作者**：Smith A, et al.
**摘要**：本研究在HEK293细胞中成功表达GALR4重组蛋白，并通过配体结合实验证实其与甘丙肽的高亲和力结合，揭示了该受体在细胞内cAMP信号通路中的抑制作用。
2. **标题**：*Optimization of Soluble GALR4 Production in E. coli for Structural Studies*
**作者**：Zhang L, et al.
**摘要**：通过优化表达载体和培养条件，在大肠杆菌中实现了可溶性GALR4重组蛋白的高效表达，为后续的X射线晶体学研究奠定基础。
3. **标题**：*Cryo-EM Structure of GALR4-G Protein Complex Reveals Activation Mechanism*
**作者**：Johnson R, et al.
**摘要**：利用冷冻电镜技术解析了GALR4与Gi蛋白复合物的三维结构，阐明了受体激活后构象变化及下游信号传导的分子机制。
4. **标题**：*Therapeutic Potential of GALR4 Agonists in Obesity Models*
**作者**：Lee S, et al.
**摘要**：基于重组GALR4蛋白筛选的小分子激动剂在肥胖小鼠模型中显示出抑制食欲和改善代谢指标的效果，提示其作为抗肥胖药物的潜力。
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**注意**：以上为模拟示例，非真实文献。建议通过以下途径获取真实文献：
- 在 **PubMed**(https://pubmed.ncbi.nlm.nih.gov/)或 **Google Scholar** 中搜索关键词：*GALR4 recombinant protein expression*, *Galanin receptor 4 structure/function*。
- 查阅《Journal of Biological Chemistry》《Biochemical Pharmacology》等期刊的相关研究。
**Background of GALR4 Recombinant Protein**
Galanin receptor type 4 (GALR4) is a G protein-coupled receptor (GPCR) that binds galanin, a neuropeptide involved in diverse physiological processes, including appetite regulation, nociception, mood modulation, and neuroendocrine functions. As one of three identified galanin receptor subtypes (GALR1. GALR2. GALR3), GALR4 shares structural homology with the GPCR family but exhibits distinct ligand-binding and signaling properties. GALR4 is primarily coupled to inhibitory G proteins (Gi/o), leading to reduced intracellular cAMP levels upon activation. While GALR4 expression is less well-characterized compared to other subtypes, studies suggest its presence in the central nervous system (e.g., hypothalamus, amygdala) and peripheral tissues, such as the pancreas and gastrointestinal tract, implicating roles in metabolic and digestive regulation.
Recombinant GALR4 protein is engineered for *in vitro* studies to elucidate its signaling mechanisms, ligand interactions, and therapeutic potential. Produced via heterologous expression systems (e.g., mammalian or insect cells), the recombinant protein retains functional domains, including extracellular ligand-binding regions and transmembrane helices. Tagged versions (e.g., His-tag, FLAG) facilitate purification and detection. Research applications include screening galanin analogs or small molecules for drug development, studying receptor dimerization, and mapping downstream pathways.
Dysregulation of galanin signaling is linked to metabolic disorders, chronic pain, and neurodegenerative diseases. GALR4-specific ligands could offer targeted therapies, though challenges remain in achieving subtype selectivity due to high homology among galanin receptors. Current studies aim to clarify GALR4’s physiological roles and validate its candidacy as a drug target, leveraging recombinant protein tools to bridge structural insights with functional outcomes.
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