| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SST |
| Uniprot No | P61278 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 89-116aa |
| 氨基酸序列 | SA NSNPAMAPRE RKAGCKNFFW KTFTSC |
| 预测分子量 | 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篇与SST(生长抑素)重组蛋白相关的文献示例(注：部分信息为模拟学术研究场景，仅供参考)：
1. **《High-level expression and purification of recombinant human somatostatin in Escherichia coli》**
- **作者**: Zhang L, et al.
- **摘要**: 本研究优化了人源生长抑素(SST)在大肠杆菌中的重组表达系统，通过融合标签技术提高可溶性表达，并利用亲和层析纯化获得高纯度蛋白。实验证实重组SST在体外抑制生长激素分泌的活性与天然蛋白一致。
2. **《Functional characterization of a novel recombinant somatostatin analog for targeted cancer therapy》**
- **作者**: Wang Y, et al.
- **摘要**: 开发了一种新型SST重组类似物，通过哺乳动物细胞表达系统生产，具有延长半衰期的修饰。该蛋白在肿瘤模型中显示出特异性结合生长抑素受体(SSTR)并抑制细胞增殖的效果，为癌症靶向治疗提供潜在策略。
3. **《Development of a rapid immunoassay for SST detection using recombinant protein-based antibodies》**
- **作者**: Gupta S, et al.
- **摘要**: 利用重组SST蛋白作为抗原，制备了单克隆抗体并建立了一种高灵敏度免疫检测方法。该技术可应用于临床样本中SST水平的定量分析，为内分泌疾病诊断提供工具。
4. **《Cryo-EM structure of the human somatostatin receptor 5 in complex with recombinant SST-28》**
- **作者**: Li H, et al.
- **摘要**: 通过冷冻电镜解析了重组SST-28蛋白与其受体SSTR5的复合物结构，揭示了配体-受体结合的关键位点，为设计靶向SSTR的药物提供了结构基础。
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**说明**：以上文献为示例性内容，实际研究中建议通过PubMed、Web of Science等平台检索真实文献(关键词：somatostatin recombinant protein, SST expression, SSTR signaling)。
**Background of SST Recombinant Proteins**
Somatostatin (SST), a cyclic neuropeptide discovered in 1973. plays a critical role in regulating endocrine and exocrine secretion. It exists in two bioactive forms (14- and 28-amino acid variants) and exerts its effects by binding to five G protein-coupled receptors (SSTR1-5). SST inhibits the release of hormones such as growth hormone, insulin, glucagon, and gastrin, making it a key modulator of metabolic homeostasis, neurotransmission, and cell proliferation.
The therapeutic potential of SST has driven interest in developing stable analogs and recombinant forms. Native SST has a short half-life (<3 minutes), limiting clinical utility. Recombinant DNA technology enables large-scale production of SST analogs with improved stability and receptor specificity. For example, octreotide and lanreotide—long-acting SST analogs—are widely used to treat acromegaly and neuroendocrine tumors.
Recombinant SST proteins are typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems. Advances in protein engineering, such as PEGylation or fusion strategies, further enhance pharmacokinetics. Additionally, recombinant SST serves as a tool for studying SSTR signaling pathways, drug discovery, and diagnostic imaging (e.g., radiolabeled SST analogs for tumor localization).
Current research focuses on optimizing receptor subtype selectivity and exploring novel applications, including targeted drug delivery and combination therapies. As a versatile biomolecule, recombinant SST continues to bridge gaps between endocrinology, oncology, and biotechnology, offering promising avenues for precision medicine.
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