| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GP9 |
| Uniprot No | P14770 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-177aa |
| 氨基酸序列 | MPAWGALFLLWATAEATKDCPSPCTCRALETMGLWVDCRGHGLTALPALPARTRHLLLANNSLQSVPPGAFDHLPQLQTLDVTQNPWHCDCSLTYLRLWLEDRTPEALLQVRCASPSLAAHGPLGRLTGYQLGSCGWQLQASWVRPGVLWDVALVAVAALGLALLAGLLCATTEALD |
| 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GP9重组蛋白的3篇参考文献示例(注：文献信息为虚拟示例，仅供参考)：
1. **文献名称**：*Structural Characterization of Recombinant GP9 in Platelet Glycoprotein Ib-IX Complex*
**作者**：Smith A, et al.
**摘要**：研究通过重组表达技术获得了GP9蛋白，结合冷冻电镜解析了其与GP1bα、GP1bβ形成的复合物结构，揭示了GP9在维持复合物稳定性中的关键作用。
2. **文献名称**：*Expression and Functional Analysis of Recombinant GP9 in a Mammalian Cell System*
**作者**：Zhang L, et al.
**摘要**：报道了在CHO细胞中高效表达重组GP9蛋白的方法，并验证其与GP1bα/β的相互作用，证实重组GP9恢复血小板粘附功能的能力。
3. **文献名称**：*Role of Recombinant GP9 in a Mouse Model of Bernard-Soulier Syndrome*
**作者**：Tanaka K, et al.
**摘要**：利用腺病毒载体递送重组GP9基因至Bernard-Soulier综合征模型小鼠，成功改善血小板减少和出血表型，为基因治疗提供依据。
4. **文献名称**：*GP9 Mutations and Recombinant Protein-based Therapeutic Strategies*
**作者**：Wang Y, et al.
**摘要**：分析了GP9基因突变导致血小板功能障碍的机制，并开发基于重组GP9的蛋白替代疗法，体外实验显示可恢复血小板聚集功能。
(注：以上文献为生成示例，实际研究中请通过PubMed、Web of Science等平台检索真实文献。)
**Background of GP9 Recombinant Protein**
Glycoprotein IX (GP9) is a critical subunit of the platelet membrane glycoprotein Ib-IX-V complex, essential for normal hemostasis. Encoded by the *GP9* gene located on chromosome 3q21.3. this 177-amino-acid protein forms a disulfide-linked complex with GP1bα and GP1bβ, mediating platelet adhesion to von Willebrand factor (VWF) at sites of vascular injury. This interaction initiates platelet activation and aggregation, playing a pivotal role in thrombosis and止血.
Mutations in *GP9* are linked to Bernard-Soulier syndrome (BSS), a rare autosomal recessive bleeding disorder characterized by macrothrombocytopenia and impaired platelet function. Studying GP9's structure-function relationships has driven the development of recombinant GP9 protein, typically produced via mammalian expression systems (e.g., CHO cells) or bacterial systems. Recombinant GP9 retains functional epitopes, enabling research into its role in platelet biology, disease modeling, and drug screening.
In therapeutic contexts, recombinant GP9 is explored for restoring platelet function in BSS through gene therapy or protein replacement strategies. It also serves as a tool for developing antiplatelet therapies targeting the GPIb-IX-V complex, relevant in thrombotic disorders. Advances in structural biology, such as cryo-EM, have refined understanding of GP9's conformational dynamics, aiding the design of targeted biologics.
Overall, GP9 recombinant protein bridges basic research and clinical innovation, offering insights into platelet pathologies and paving the way for novel treatments in hematology and beyond.
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