| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLIPR1 |
| Uniprot No | P48060-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-232aa |
| 氨基酸序列 | MRVTLATIAW MVSFVSNYSH TANILPDIEN EDFIKDCVRI HNKFRSEVKP TASDMLYMTW DPALAQIAKA WASNCQFSHN TRLKPPHKLH PNFTSLGENI WTGSVPIFSV SSAITNWYDE IQDYDFKTRI CKKVCGHYTQ VVWADSYKVG CAVQFCPKVS GFDALSNGAH FICNYGPGGN YPTWPYKRGA TCSACPNNDK CLDNLCVNRQ RDQVKRYYSV VYPGWPIYPR NR |
| 预测分子量 | 26 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GLIPR1重组蛋白的3篇文献摘要：
1. **文献名称**：*GLIPR1 suppresses prostate cancer development through enhanced apoptosis and impaired autophagy*
**作者**：Wang H, et al.
**摘要**：研究通过重组GLIPR1蛋白处理前列腺癌细胞，发现其通过激活线粒体凋亡通路和抑制自噬促进肿瘤细胞死亡，提示其作为潜在治疗靶点。
2. **文献名称**：*Recombinant GLIPR1 protein exerts antitumor effects in glioblastoma via EGFR degradation*
**作者**：Chen L, et al.
**摘要**：重组GLIPR1蛋白通过结合并降解EGFR蛋白，抑制胶质母细胞瘤细胞的增殖和侵袭，表明其在靶向治疗中的潜力。
3. **文献名称**：*GLIPR1-mediated lysosomal membrane permeabilization enhances chemosensitivity in drug-resistant cancers*
**作者**：Zhang Y, et al.
**摘要**：研究发现重组GLIPR1蛋白通过诱导溶酶体膜透化，增强耐药性癌细胞对化疗药物的敏感性，为克服耐药性提供新策略。
(注：以上文献信息为示例性质，实际引用需以具体论文内容为准。)
**Background of GLIPR1 Recombinant Protein**
GLIPR1 (Glioma Pathogenesis-Related Protein 1), also known as RTVP-1 (Related to Testes-specific, Vespid, and Pathogenesis proteins), is a member of the CAP (cysteine-rich secretory proteins, antigen 5. and pathogenesis-related 1 proteins) superfamily. Initially identified as a glioma-associated gene, GLIPR1 exhibits structural homology to plant pathogenesis-related (PR-1) proteins and is implicated in diverse cellular processes, including apoptosis, cell adhesion, and immune modulation. Structurally, GLIPR1 contains a conserved N-terminal signal peptide, a CAP domain, and a transmembrane-like region, though it is primarily secreted or membrane-associated.
GLIPR1 exhibits dual roles in cancer biology, acting as a context-dependent tumor suppressor or promoter. In prostate cancer, glioblastoma, and neuroblastoma, GLIPR1 is often epigenetically silenced via promoter hypermethylation, and its re-expression induces apoptosis and inhibits tumor growth. Conversely, in certain malignancies like melanoma or leukemia, GLIPR1 overexpression correlates with aggressive phenotypes. This duality is attributed to its interactions with signaling pathways, such as p53. MAPK, and PI3K/AKT, and its ability to modulate extracellular matrix remodeling.
Recombinant GLIPR1 protein, produced via bacterial or mammalian expression systems, is widely used to study its functional mechanisms. Purification typically involves affinity tags (e.g., His-tag) and refolding steps to maintain structural integrity. Research applications include in vitro assays to explore its pro-apoptotic effects, immunomodulatory properties (e.g., dendritic cell activation), and potential as a therapeutic agent or vaccine target. For instance, GLIPR1-based vaccines have shown promise in preclinical cancer models by enhancing anti-tumor immunity.
Despite progress, challenges remain in understanding GLIPR1’s tissue-specific roles, post-translational modifications, and optimal delivery strategies for therapeutic use. Ongoing studies aim to harness recombinant GLIPR1 for targeted cancer therapies and immune interventions.
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