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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTN |
| Uniprot No | P21246 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-168aa |
| 氨基酸序列 | MGKKEKPEKK VKKSDCGEWQ WSVCVPTSGD CGLGTREGTR TGAECKQTMK TQRCKIPCNW KKQFGAECKY QFQAWGECDL NTALKTRTGS LKRALHNAEC QKTVTISKPC GKLTKPKPQA ESKKKKKEGK KQEKMLD |
| 预测分子量 | 19 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PTN(多效生长因子，Pleiotrophin)重组蛋白的3篇参考文献示例，涵盖其表达、功能及应用研究：
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1. **文献名称**：*Expression and Purification of Recombinant Human Pleiotrophin in Escherichia coli*
**作者**：Chen L, Wang Y, et al.
**摘要**：该研究报道了利用大肠杆菌表达系统高效生产重组人源PTN蛋白的方法。通过优化密码子、诱导条件及纯化步骤，成功获得高纯度且具有生物活性的PTN蛋白，为后续功能研究奠定基础。
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2. **文献名称**：*Pleiotrophin Enhances Neurite Outgrowth via Glypican-Mediated Signaling Pathways*
**作者**：Meng X, Liu H, et al.
**摘要**：研究探讨了PTN重组蛋白在神经再生中的作用，发现其通过结合细胞表面受体Glypican-1激活下游信号通路，显著促进体外培养的神经元突触生长，提示其在神经损伤修复中的潜在应用价值。
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3. **文献名称**：*Targeting Pleiotrophin in Glioblastoma: Recombinant Protein Suppresses Tumor Angiogenesis*
**作者**：Kim S, Park JH, et al.
**摘要**：该研究利用PTN重组蛋白进行胶质母细胞瘤治疗实验，发现其通过抑制VEGF信号通路减少肿瘤血管生成，显著延缓小鼠模型中肿瘤生长，为PTN在抗肿瘤治疗中的机制提供了新见解。
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(注：以上文献信息为模拟示例，实际引用需以具体数据库检索结果为准。)
**Background of PTN Recombinant Protein**
Pleiotrophin (PTN), also known as heparin-binding growth factor 8 (HBGF-8), is a secreted cytokine belonging to the heparin-binding growth factor family. It plays critical roles in diverse physiological and pathological processes, including cell proliferation, migration, differentiation, and angiogenesis. PTN is highly expressed during embryonic development but shows limited expression in healthy adult tissues. Its upregulation is observed in various cancers (e.g., glioblastoma, melanoma, breast cancer) and inflammatory conditions, linking it to tumorigenesis, metastasis, and tissue remodeling.
Recombinant PTN protein is produced using recombinant DNA technology, where the PTN gene is cloned into expression vectors (e.g., bacterial, mammalian, or insect cell systems) to enable large-scale, high-purity protein production. This approach ensures consistency and scalability, which are essential for research and therapeutic applications.
Functionally, PTN interacts with cell surface receptors such as receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) and neuropilins, activating downstream signaling pathways like PI3K/Akt, MAPK, and Wnt/β-catenin. These pathways regulate cell survival, differentiation, and angiogenesis. In neuroscience, PTN promotes neurite outgrowth, axonal guidance, and neuronal survival, highlighting its neurotrophic properties.
PTN recombinant protein is widely used in biomedical research to study its role in cancer progression, neuroregeneration, and tissue repair. It also holds potential as a therapeutic target; for instance, inhibiting PTN signaling may suppress tumor growth, while its neuroprotective effects could aid in treating neurodegenerative diseases. Additionally, PTN is explored in tissue engineering for its ability to enhance stem cell differentiation and tissue regeneration.
Structurally, PTN is a 18-20 kDa protein with two conserved heparin-binding domains stabilized by disulfide bonds. Recombinant variants often include tags (e.g., His-tag) for purification and are validated via mass spectrometry and bioactivity assays to ensure functional integrity.
In summary, PTN recombinant protein serves as a vital tool for unraveling PTN's multifunctional biology and advancing therapeutic strategies in oncology, neurology, and regenerative medicine.
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