纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | F10 |
Uniprot No | P00742 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 41-488aa |
氨基酸序列 | ANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK |
预测分子量 | 57.8 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F10(凝血因子X)重组蛋白的3篇代表性文献示例:
1. **文献名称**:*Recombinant human factor X: high yield production and structural properties*
**作者**:M. Krishnaswamy et al.
**摘要**:研究报道了通过哺乳动物细胞表达系统高效生产重组人凝血因子X(rF10)的方法,并分析了其结构与天然因子的相似性,证实其具备正常的钙离子依赖性和酶原激活特性。
2. **文献名称**:*Functional characterization of recombinant factor X variants in coagulation assays*
**作者**:J. P. Smith et al.
**摘要**:通过体外凝血实验评估重组F10的功能,发现其与血浆来源的F10在凝血酶生成和凝血时间调节中表现一致,支持其作为替代治疗药物的潜力。
3. **文献名称**:*Engineering recombinant factor X for improved stability and activity*
**作者**:L. Chen & R. G. DiCarlo
**摘要**:通过定点突变技术对重组F10进行改造,增强了其热稳定性和抗凝血酶抑制能力,为开发长效型凝血因子制剂提供了新策略。
注:以上文献信息为示例性质,实际引用需根据具体研究内容检索PubMed、Web of Science等数据库获取真实文献。
F10 recombinant protein, commonly referred to as recombinant human coagulation Factor X (FX), is a critical component in the blood coagulation cascade. Factor X is a vitamin K-dependent serine protease that plays a central role in both the intrinsic and extrinsic coagulation pathways, where it is activated to Factor Xa (FXa) by either the Factor IXa-Factor VIIIa complex or the tissue factor-Factor VIIa complex. Once activated, FXa interacts with Factor Va, calcium ions, and phospholipid surfaces to form the prothrombinase complex, which converts prothrombin to thrombin—a pivotal step in fibrin clot formation.
The recombinant version of Factor X is produced using biotechnological methods, typically in mammalian expression systems such as Chinese hamster ovary (CHO) cells. These systems enable post-translational modifications, including γ-carboxylation of glutamic acid residues, which are essential for the protein’s membrane-binding and functional activity. Recombinant F10 offers advantages over plasma-derived Factor X, including reduced risk of pathogen transmission, batch-to-batch consistency, and scalability for industrial production.
F10 recombinant protein has significant applications in biomedical research and therapeutic development. It is used to study coagulation disorders, screen anticoagulant drugs, and engineer biosensors for real-time monitoring of clotting processes. Additionally, it serves as a critical reagent in bypass therapies for hemophilia patients with inhibitors. Recent advances in protein engineering have also explored modified F10 variants with enhanced stability or altered substrate specificity for targeted therapeutic interventions. Its role in hemostasis and thrombosis continues to make it a focal point in hematology and drug discovery.
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