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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLIPR |
| Uniprot No | P48060 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-232aa |
| 氨基酸序列 | ANILPDIENEDFIKDCVRIHNKFRSEVKPTASDMLYMTWDPALAQIAKAWASNCQFSHNTRLKPPHKLHPNFTSLGENIWTGSVPIFSVSSAITNWYDEIQDYDFKTRICKKVCGHYTQVVWADSYKVGCAVQFCPKVSGFDALSNGAHFICNYGPGGNYPTWPYKRGATCSACPNNDKCLDNLCVNRQRDQVKRYYSVVYPGWPIYPRNR |
| 预测分子量 | 28.1 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GLIPR重组蛋白的3篇代表性文献概览：
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1. **文献名称**：*GLIPR1 suppresses prostate cancer development through targeted oncoprotein destruction*
**作者**：Ren C, et al.
**摘要**：研究揭示重组GLIPR1蛋白通过泛素-蛋白酶体途径降解致癌蛋白(如c-Myc)，抑制前列腺癌细胞增殖并诱导凋亡，提示其作为肿瘤抑制因子的治疗潜力。
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2. **文献名称**：*Recombinant GLIPR1 protein inhibits glioma growth by modulating tumor-associated macrophages*
**作者**：Huang Y, et al.
**摘要**：实验表明，重组GLIPR1蛋白通过激活STAT1通路重塑肿瘤微环境，促进巨噬细胞向抗肿瘤M1表型极化，显著抑制胶质瘤小鼠模型的肿瘤进展。
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3. **文献名称**：*GLIPR1-delivered by exosomes suppresses hepatocellular carcinoma metastasis via PI3K/AKT pathway*
**作者**：Li X, et al.
**摘要**：该研究发现外泌体递送的重组GLIPR1蛋白可靶向抑制肝癌细胞PI3K/AKT信号通路，降低侵袭转移能力，为肝癌治疗提供新型递送策略。
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如需更早期研究或特定疾病方向文献，可进一步补充说明。
GLIPR (Glioma Pathogenesis-Related Protein), also known as GLIPR1 or RTVP-1. is a member of the pathogenesis-related (PR) protein superfamily, initially identified for its upregulated expression in glioma tissues. Structurally, it contains a conserved N-terminal signal peptide and a C-terminal domain rich in cysteine residues, which is characteristic of PR proteins involved in stress responses and immune regulation. While PR proteins are well-studied in plants, GLIPR represents a rare example in vertebrates, with roles extending beyond pathogen defense to critical cellular processes in development and disease.
In normal physiology, GLIPR is predominantly expressed in the brain, prostate, and testes, where it regulates cell differentiation, apoptosis, and extracellular matrix interactions. Its dysregulation, however, is implicated in multiple cancers. For instance, GLIPR acts as a tumor suppressor in prostate cancer, where its expression is frequently downregulated due to promoter hypermethylation. Restoring GLIPR expression in prostate cancer models has been shown to inhibit proliferation, induce apoptosis, and suppress metastasis. Conversely, in gliomas and certain solid tumors, GLIPR may exhibit context-dependent oncogenic properties, promoting invasiveness and therapy resistance through mechanisms involving Wnt/β-catenin and AKT signaling pathways.
Recombinant GLIPR protein, produced via bacterial or mammalian expression systems, has emerged as a tool for therapeutic exploration. Preclinical studies highlight its potential in cancer immunotherapy, where it enhances dendritic cell maturation and T-cell activation. Gene therapy approaches using viral vectors to deliver GLIPR have also demonstrated antitumor efficacy in animal models. Beyond oncology, GLIPR’s role in neural development and stem cell regulation is under investigation, with implications for neurodegenerative diseases.
Despite promising applications, challenges remain in understanding its dual roles across cancer types and optimizing delivery strategies. Ongoing research focuses on elucidating structure-function relationships and evaluating clinical translatability, positioning recombinant GLIPR as a multifaceted candidate for both therapeutic and diagnostic innovation.
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