| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPC |
| Uniprot No | P04921 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-57aa |
| 氨基酸序列 | ADPMWSTRSPNSTAWPLSLEPDPGMASASTTMHTTTIAEPDPGMSGWPDG RMETSTPTIMHHHHHH |
| 预测分子量 | 7 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3篇关于GPC(Glypican)重组蛋白的参考文献摘要，涵盖其在癌症、病毒研究及信号传导中的应用：
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1. **文献名称**：*Recombinant human glypican-3 stimulates proliferation of primary hepatocytes in vitro*
**作者**：Li, Y., et al.
**摘要**：研究报道了通过大肠杆菌表达系统重组表达人源Glypican-3(GPC3)蛋白，并验证其刺激原代肝细胞增殖的能力，揭示了GPC3在肝癌发生中的潜在作用机制。
2. **文献名称**：*Structural characterization of recombinant GPC1 and its role in Wnt signaling regulation*
**作者**：Chen, X., et al.
**摘要**：利用昆虫细胞表达系统制备重组Glypican-1(GPC1)，通过晶体学解析其结构，并证明其通过结合Wnt蛋白调控细胞信号传导，为靶向GPC1的癌症治疗提供依据。
3. **文献名称**：*Recombinant GPC of Lassa virus as a vaccine antigen*
**作者**：Branco, L.M., et al.
**摘要**：研究通过哺乳动物细胞表达拉沙病毒(Lassa virus)的重组糖蛋白复合体(GPC)，评估其作为疫苗抗原的免疫原性，展示其在动物模型中诱导中和抗体的效果。
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注：以上文献为示例，实际引用需根据具体研究领域核实原文。若需扩展，可补充GPC3在靶向疗法或重组蛋白纯化技术的文献。
**Background of GPC Recombinant Proteins**
Glypican (GPC) is a family of heparan sulfate (HS)-linked proteoglycans anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) moiety. These proteins play critical roles in regulating cellular signaling pathways, including Hedgehog, Wnt, and fibroblast growth factor (FGF) signaling, by modulating ligand-receptor interactions. The GPC family comprises six members (GPC1–GPC6) in mammals, each exhibiting tissue-specific expression patterns and involvement in developmental processes, tissue homeostasis, and disease pathogenesis. Dysregulation of GPCs has been linked to cancers, genetic disorders like Simpson-Golabi-Behmel syndrome, and metabolic diseases.
Recombinant GPC proteins are engineered to study their structure-function relationships, therapeutic potential, and diagnostic applications. Produced using heterologous expression systems (e.g., mammalian cells, bacteria, or insect cells), these proteins retain key functional domains, such as the HS chains and core protein motifs, while enabling scalable purification. Mammalian systems (e.g., CHO or HEK293 cells) are preferred for preserving post-translational modifications like HS glycosylation, critical for biological activity.
GPC recombinant proteins are widely used in drug discovery, particularly in oncology. For example, GPC3 is overexpressed in hepatocellular carcinoma and serves as a target for antibody-based therapies and CAR-T cells. Structural studies using recombinant GPCs have elucidated HS-binding mechanisms and interactions with growth factors. Additionally, they are employed as diagnostic tools to detect autoantibodies in diseases or as standards in biomarker assays.
Challenges in GPC recombinant production include maintaining HS chain heterogeneity and avoiding aggregation. Advances in glycoengineering and purification techniques continue to address these limitations, enhancing their utility in biomedical research and therapeutic development. Overall, GPC recombinant proteins bridge basic science and clinical innovation, offering insights into disease mechanisms and enabling precision medicine approaches.
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