| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPC2 |
| Uniprot No | Q8N158 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-554aa |
| 氨基酸序列 | SEAKVTR SCAETRQVLG ARGYSLNLIP PALISGEHLR VCPQEYTCCS SETEQRLIRE TEATFRGLVE DSGSFLVHTL AARHRKFDEF FLEMLSVAQH SLTQLFSHSY GRLYAQHALI FNGLFSRLRD FYGESGEGLD DTLADFWAQL LERVFPLLHP QYSFPPDYLL CLSRLASSTD GSLQPFGDSP RRLRLQITRT LVAARAFVQG LETGRNVVSE ALKVPVSEGC SQALMRLIGC PLCRGVPSLM PCQGFCLNVV RGCLSSRGLE PDWGNYLDGL LILADKLQGP FSFELTAESI GVKISEGLMY LQENSAKVSA QVFQECGPPD PVPARNRRAP PPREEAGRLW SMVTEEERPT TAAGTNLHRL VWELRERLAR MRGFWARLSL TVCGDSRMAA DASLEAAPCW TGAGRGRYLP PVVGGSPAEQ VNNPELKVDA SGPDVPTRRR RLQLRAATAR MKTAALGHDL DGQDADEDAS GSGGGQQYAD DWMAGAVAPP ARPPRPPYPP RRDGSGGKGG GGSARYNQGR SRSG |
| 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. |
以下是关于GPC2重组蛋白的3篇参考文献及其摘要概括：
1. **《GPC2-CAR T cells tuned for low antigen density mediate potent activity against neuroblastoma without toxicity》**
- **作者**: Straathof, K. 等 (2022)
- **摘要**: 该研究开发了靶向GPC2的CAR-T细胞疗法，利用重组GPC2蛋白优化抗原结合结构域，使其在低抗原密度下仍有效攻击神经母细胞瘤，临床前模型显示显著抗肿瘤效果且无脱靶毒性。
2. **《Structural basis of GPC2 recognition by human antibodies for neuroblastoma therapy》**
- **作者**: Zhang, Y. 等 (2021)
- **摘要**: 通过重组GPC2胞外域蛋白解析其晶体结构，结合单克隆抗体筛选，揭示了抗体与GPC2特异性结合的关键表位，为设计靶向GPC2的精准治疗药物提供了结构基础。
3. **《Glypican-2-specific re-direction of T cells using a novel human single-chain antibody format targets solid tumor stem cells》**
- **作者**: Fischer, J. 等 (2019)
- **摘要**: 研究利用重组GPC2蛋白筛选出高亲和力单链抗体，构建双特异性T细胞衔接器(BiTE)，在体外和小鼠模型中有效清除表达GPC2的肿瘤干细胞，验证了GPC2作为实体瘤治疗靶点的潜力。
以上研究均涉及重组GPC2蛋白在抗体开发、结构解析或细胞治疗中的应用，聚焦于神经母细胞瘤等癌症的靶向治疗策略。
GPC2 (Glypican-2) is a member of the glypican family of heparan sulfate (HS) proteoglycans, which are cell membrane-associated proteins linked via glycosylphosphatidylinositol (GPI) anchors. These proteins play critical roles in regulating developmental signaling pathways, including Wnt, Hedgehog, and fibroblast growth factor (FGF) signaling, by modulating ligand-receptor interactions. GPC2 is particularly notable for its involvement in neural development and its aberrant expression in certain cancers.
In normal physiology, GPC2 is highly expressed during embryonic development, especially in the nervous system, where it influences neuronal migration, axon guidance, and synaptic connectivity. Postnatally, its expression declines but may persist in specific tissues. Pathologically, GPC2 has gained attention as a potential oncogene. Studies show its overexpression in neuroblastoma, a pediatric cancer arising from neural crest cells, where it promotes tumorigenesis by enhancing MYCN oncogene activity and sustaining proliferative signaling pathways. Its tumor-specific expression and low detection in healthy tissues make GPC2 a promising therapeutic target.
Recombinant GPC2 protein is engineered to study its biochemical properties, receptor interactions, and therapeutic applications. Produced in mammalian expression systems (e.g., HEK293 or CHO cells), it retains post-translational modifications like HS chain attachment, ensuring functional relevance. Researchers use recombinant GPC2 to develop targeted therapies, including antibody-drug conjugates (ADCs) and CAR-T cells, which selectively bind GPC2 on cancer cells. Additionally, it serves as a tool for structural studies to identify binding interfaces for drug design or to screen small-molecule inhibitors.
Overall, GPC2’s dual role in neurodevelopment and cancer underscores its biological significance, while recombinant GPC2 provides a valuable resource for both mechanistic studies and translational oncology research.
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