| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | F5 |
| Uniprot No | P30939 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-366aa |
| 氨基酸序列 | MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC |
| 预测分子量 | 41,7 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F5(凝血因子V)重组蛋白的相关文献摘要整理：
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1. **文献名称**: *"Recombinant factor V as a novel bypass agent in haemophilia"*
**作者**: Smith J et al.
**摘要**: 研究探讨重组F5蛋白作为旁路剂治疗血友病患者的潜在疗效，证明其通过增强凝血酶生成改善止血功能，为抑制物阳性患者提供新治疗策略。
2. **文献名称**: *"Structural and functional characterization of recombinant human factor V"*
**作者**: Chen L & Dahlbäck B.
**摘要**: 通过X射线晶体学分析重组人F5的结构，揭示其与凝血酶和磷脂膜的相互作用机制，为理解其促凝活性提供分子基础。
3. **文献名称**: *"Expression and purification of bioactive recombinant factor V in mammalian cells"*
**作者**: Gupta R et al.
**摘要**: 开发基于HEK293细胞的高效重组F5蛋白表达系统，验证其生物活性与天然因子V相当，优化后的纯化流程为大规模生产奠定基础。
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**注**：以上文献为示例性质，实际研究中建议通过PubMed或Web of Science检索最新论文，关键词包括“recombinant factor V”或“F5 protein therapeutics”。
**Background of Recombinant Factor V (F5) Protein**
Factor V (FV), a critical glycoprotein in the blood coagulation cascade, was first identified in the mid-20th century as a key component of the prothrombinase complex. Native FV is synthesized in the liver and circulates in plasma as an inactive precursor. Upon activation by thrombin or Factor Xa, it becomes Factor Va (FVa), a cofactor that significantly enhances the conversion of prothrombin to thrombin by Factor Xa, calcium ions, and phospholipid surfaces. This process is vital for effective clot formation.
The molecular structure of FV includes multiple domains (A1-A3. B, and C1-C2) that mediate interactions with other coagulation factors and cell membranes. Genetic mutations in the F5 gene, such as the Factor V Leiden variant, are linked to thrombotic disorders, highlighting its physiological and pathological relevance.
Recombinant Factor V (rFV) emerged with advances in biotechnology to address limitations of plasma-derived FV, including supply shortages and infection risks. Produced via genetic engineering in mammalian cell systems (e.g., CHO or HEK293 cells), rFV mirrors the structure and function of native FV. Its development leverages codon optimization, post-translational modification, and purification techniques to ensure stability and activity.
Clinically, rFV has potential applications in treating rare bleeding disorders, such as Factor V deficiency, and in reversing anticoagulant effects. Research also explores its role in improving thrombin generation assays or as a component in bypassing agents for hemophilia patients with inhibitors. While no recombinant FV product is yet FDA-approved, ongoing studies aim to optimize its efficacy and safety profile.
Overall, recombinant F5 represents a convergence of coagulation biology and biomanufacturing innovation, offering tailored therapeutic solutions and enhancing our understanding of hemostasis.
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