| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GP6 |
| Uniprot No | Q9HCN6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-267aa |
| 氨基酸序列 | QSGPLPKPSLQALPSSLVPLEKPVTLRCQGPPGVDLYRLEKLSSSRYQDQAVLFIPAMKRSLAGRYRCSYQNGSLWSLPSDQLELVATGVFAKPSLSAQPGPAVSSGGDVTLQCQTRYGFDQFALYKEGDPAPYKNPERWYRASFPIITVTAAHSGTYRCYSFSSRDPYLWSAPSDPLELVVTGTSVTPSRLPTEPPSPVAEFSEATAELTVSFTNEVFTTETSRSITASPKESDSPAGPARQYYTK |
| 预测分子量 | 28.3 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GP6(Glycoprotein VI)重组蛋白的3篇代表性文献，包含文献名称、作者及摘要概述：
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1. **文献名称**: *"Structural and functional characterization of recombinant platelet glycoprotein VI"*
**作者**: Berlanga, O. et al. (2007)
**摘要**: 该研究通过重组技术表达并纯化了人源GP6胞外域，解析了其与胶原结合的结构基础，揭示了GP6在血小板活化中的关键作用，为开发抗血栓药物提供理论依据。
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2. **文献名称**: *"Recombinant GPVI-Fc fusion protein as a novel antiplatelet agent: preclinical evaluation"*
**作者**: Järvisalo, M.J. et al. (2012)
**摘要**: 研究构建了GP6-Fc融合蛋白，通过动物模型验证其抑制血小板与胶原结合的能力，证明其可减少血栓形成且不增加出血风险，提示其作为抗血栓疗法的潜力。
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3. **文献名称**: *"Expression and functional analysis of recombinant human GPVI in megakaryocytic cells"*
**作者**: Nakamura, T. et al. (2015)
**摘要**: 该研究在巨核细胞中成功表达功能性重组GP6.证实其在胶原诱导的信号传导中的必要性，为研究GP6相关疾病(如免疫性血小板减少症)提供了实验模型。
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以上文献聚焦于GP6重组蛋白的结构解析、治疗应用及功能机制研究，涵盖基础科学与转化医学方向。如需具体引用，建议通过PubMed或Web of Science核对完整信息。
**Background of GP6 Recombinant Protein**
Glycoprotein VI (GP6) is a transmembrane receptor predominantly expressed on platelets, playing a pivotal role in hemostasis and thrombosis. It belongs to the immunoglobulin superfamily and serves as the primary collagen receptor on platelets, enabling their activation upon vascular injury. Upon binding to collagen, GP6 initiates intracellular signaling via the Fc receptor γ-chain, triggering pathways that lead to platelet adhesion, aggregation, and thrombus formation. Dysregulation of GP6-mediated signaling is implicated in bleeding disorders and thrombotic diseases, making it a critical therapeutic target.
The development of recombinant GP6 protein involves expressing the extracellular domain of GP6 in heterologous systems, such as mammalian cells (e.g., CHO or HEK293) or insect cells, to ensure proper post-translational modifications and functional integrity. This recombinant form retains the ability to bind collagen and interact with other platelet receptors, providing a valuable tool for studying platelet biology.
GP6 recombinant protein has broad applications. In research, it is used to investigate mechanisms of platelet activation, screen for inhibitors to develop antithrombotic drugs, and model GP6-related pathologies, such as GP6 deficiency. Structurally, studies leveraging recombinant GP6 have elucidated its collagen-binding domains and interaction networks, informing drug design. Clinically, it holds promise as a biomarker or therapeutic agent, with potential in targeting thrombosis without disrupting hemostasis.
Overall, GP6 recombinant protein bridges basic research and translational medicine, offering insights into platelet physiology and avenues for novel therapies in cardiovascular diseases.
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