| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SSTR5 |
| Uniprot No | P35346 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 307-364aa |
| 氨基酸序列 | LSDNFRQSFQKVLCLRKGSGAKDADATEPRPDRIRQQQEATPPAHRAAANGLMQTSKL |
| 预测分子量 | 8.0 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. |
以下是关于SSTR5重组蛋白的3篇参考文献示例(内容基于公开研究整理，非真实文献，仅供参考)：
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1. **文献名称**：*Expression and functional characterization of recombinant human somatostatin receptor subtype 5 (SSTR5) in mammalian cells*
**作者**：Smith A, et al.
**摘要**：该研究通过将人源SSTR5基因克隆至HEK293细胞中表达重组蛋白，利用放射性配体结合实验验证其与生长抑素类似物的高亲和力结合，并证实其通过抑制cAMP信号通路调控激素分泌的功能。
2. **文献名称**：*Structural insights into SSTR5 activation and G protein coupling by cryo-EM*
**作者**：Chen L, et al.
**摘要**：通过冷冻电镜技术解析了SSTR5与天然配体及Gi蛋白复合物的三维结构，揭示了受体激活的构象变化机制，为靶向SSTR5的药物设计提供结构基础。
3. **文献名称**：*Development of a stable CHO cell line expressing human SSTR5 for high-throughput drug screening*
**作者**：Wang Y, et al.
**摘要**：研究构建了稳定表达SSTR5重组蛋白的中国仓鼠卵巢(CHO)细胞系，优化了蛋白纯化流程，并应用于高通量筛选靶向SSTR5的抗肿瘤候选化合物。
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**提示**：实际文献需通过PubMed、Google Scholar等平台检索关键词“SSTR5 recombinant protein”“somatostatin receptor 5 expression”等获取。建议结合具体研究方向筛选近年高影响力论文。
Somatostatin receptor type 5 (SSTR5) is a G protein-coupled receptor (GPCR) that binds somatostatin, a cyclic peptide hormone regulating endocrine and exocrine secretions, neurotransmission, and cell proliferation. As one of five known somatostatin receptor subtypes (SSTR1-5), SSTR5 is distinguished by its high affinity for somatostatin-28 and selective activation pathways. It is predominantly expressed in the brain, pituitary gland, pancreas, and gastrointestinal tract, where it modulates hormone release (e.g., growth hormone, insulin, glucagon) and inhibits tumor cell growth in neuroendocrine malignancies.
Recombinant SSTR5 proteins are engineered using heterologous expression systems (e.g., CHO, HEK293. or E. coli) to produce purified, functional receptors for biomedical research. These systems enable precise control of post-translational modifications, enhancing receptor stability and ligand-binding fidelity. The recombinant protein typically retains native structural features, including seven transmembrane domains and extracellular loops critical for ligand interaction.
Research on SSTR5 recombinant proteins has accelerated drug discovery, particularly for neuroendocrine tumors and acromegaly. Synthetic somatostatin analogs (e.g., octreotide, pasireotide) targeting SSTR5 are used clinically to suppress pathological hormone secretion and tumor progression. Additionally, SSTR5 serves as a molecular target for radiolabeled peptides in diagnostic imaging (e.g., PET/CT scans) and targeted radiotherapy. Recent studies also explore its role in metabolic disorders and immune regulation, broadening therapeutic potential.
Despite advancements, challenges persist in understanding SSTR5’s biased signaling mechanisms and tissue-specific interactions. Recombinant protein tools remain essential for elucidating receptor dynamics, facilitating the development of subtype-selective ligands with minimized off-target effects. This work underscores the intersection of structural biology, pharmacology, and precision medicine in targeting GPCRs like SSTR5.
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