| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GRP |
| Uniprot No | Q3ZCW2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-172aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMAGSVADSDAVVKLDDGHLNNSLSSP VQADVYFPRLIVPFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDS EDPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAIPYFPFIPDQPFRV EILCEHPRFRVFVDGHQLFDFYHRIQTLSAIDTIKINGDLQITKLG |
| 预测分子量 | 22 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GRP(Glucose-Regulated Protein，如GRP78/BiP)重组蛋白的参考文献示例(内容为模拟概括，非真实文献)：
1. **文献名称**：*GRP78重组蛋白在肿瘤细胞应激反应中的调控机制*
**作者**：Zhang et al.
**摘要**：研究通过大肠杆菌表达重组GRP78蛋白，发现其在肿瘤细胞中通过调控内质网应激通路，抑制细胞凋亡并促进耐药性，为癌症治疗提供新靶点。
2. **文献名称**：*重组GRP蛋白在糖尿病模型中的保护作用*
**作者**：Kim & Patel
**摘要**：利用哺乳动物细胞系统表达GRP94重组蛋白，实验表明其通过减轻胰岛β细胞的内质网氧化应激，改善小鼠糖尿病症状。
3. **文献名称**：*高效纯化GRP78重组蛋白的层析技术优化*
**作者**：Li et al.
**摘要**：开发了一种基于亲和层析的新型纯化方法，显著提高了GRP78重组蛋白的产量和稳定性，适用于大规模工业制备。
4. **文献名称**：*GRP75重组蛋白调控线粒体功能与神经退行性疾病*
**作者**：Wang et al.
**摘要**：通过体外实验证实，重组GRP75蛋白可增强线粒体能量代谢，延缓阿尔茨海默病模型中的神经元损伤。
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**注**：以上文献为示例性概括，实际研究中请通过PubMed、Web of Science等平台检索真实文献(关键词：GRP recombinant protein, GRP78/BiP, 重组葡萄糖调节蛋白)。
**Background of GRP Recombinant Proteins**
Gastrin-releasing peptide (GRP), a 27-amino acid neuropeptide, belongs to the bombesin-like peptide family and plays critical roles in physiological and pathological processes. Initially isolated from porcine stomach, GRP binds to the gastrin-releasing peptide receptor (GRPR), a G-protein-coupled receptor (GPCR), to regulate cellular functions such as proliferation, differentiation, and neurotransmission. Its involvement in cancer progression, particularly in autocrine signaling within tumors like lung, prostate, and breast cancers, has driven interest in GRP as a therapeutic or diagnostic target.
Recombinant GRP proteins are engineered using biotechnological platforms (e.g., *E. coli*, yeast, or mammalian cell systems*) to ensure high purity and bioactivity. These systems enable scalable production while maintaining the peptide’s structural integrity, essential for functional studies. Advances in protein engineering, such as codon optimization and fusion tags (e.g., His-tags), have improved yield and simplified purification via affinity chromatography.
GRP recombinant proteins are widely utilized in biomedical research. They serve as tools to study GRPR-mediated signaling pathways, screen potential inhibitors for cancer therapy, or develop imaging probes for tumor detection. For instance, GRP-based radiotracers are explored in PET imaging to visualize GRPR-overexpressing malignancies. Additionally, recombinant GRP aids in understanding its role in neurological processes, including itch sensation and stress responses.
Despite progress, challenges remain, such as ensuring *in vivo* stability and minimizing immunogenicity. Ongoing research focuses on modifying recombinant GRP (e.g., PEGylation) to enhance pharmacokinetics. Overall, GRP recombinant proteins bridge basic science and clinical applications, offering insights into disease mechanisms and therapeutic innovations.
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