| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | F8 |
| Uniprot No | P61647 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-398aa |
| 氨基酸序列 | MRPGGALLALLASLLLLLLLRLLWCPADAPGRARILVEESREATHGTPAALRTLRSPATAVPRATNSTYLNEKSLQLTEKCKNLQYGIESFSNKTKGYSENDYLQIITDIQSCPWKRQAEEYANFRAKLASCCDAVQNFVVSQNNTPVGTNMSYEVESKKEIPIKKNIFHMFPVSQPFVDYPYNQCAVVGNGGILNKSLCGTEIDKSDFVFRCNLPPTTGDVSKDVGSKTNLVTINPSIITLKYGNLKEKKALFLEDIATYGDAFFLLPAFSFRANTGTSFKVYYTLEESKARQKVLFFHPKYLKDLALFWRTKGVTAYRLSTGLMITSVAVELCKNVKLYGFWPFSKTVEDIPVSHHYYDNKLPKHGFHQMPKEYSQILQLHMKGILKLQFSKCEVA |
| 预测分子量 | 44,8 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F8重组蛋白(重组凝血因子VIII)的3篇代表性文献示例(内容基于公开研究整理，建议核实原文)：
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1. **文献名称**：*Efficacy and safety of a third-generation recombinant factor VIII (turoctocog alfa) in previously treated patients with severe hemophilia A*
**作者**：Kjalke M, et al.
**摘要**：该研究评估第三代重组FVIII(turoctocog alfa)在重度血友病A患者中的疗效与安全性。通过多中心临床试验发现，该重组蛋白止血有效率达92%，且未检测到抑制物抗体产生，证实其长期治疗的安全性和耐受性。
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2. **文献名称**：*Long-term safety and efficacy of recombinant factor VIII Fc fusion protein (rFVIIIFc) in hemophilia A*
**作者**：Mahlangu J, et al.
**摘要**：研究报道了Fc融合技术延长重组FVIII半衰期的效果。结果显示，rFVIIIFc的半衰期较传统重组FVIII提高1.5倍，能减少注射频率，且未增加免疫原性风险，为血友病A的预防性治疗提供新选择。
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3. **文献名称**：*Comparative analysis of recombinant FVIII products: structural variations and functional implications*
**作者**：Pipe SW, et al.
**摘要**：通过质谱和功能实验比较多种重组FVIII产品(如Kogenate®、Advate®)，发现不同细胞系(如CHO vs. BHK)生产的FVIII糖基化修饰差异可能影响其稳定性和体内活性，为优化生产工艺提供理论依据。
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**注**：以上为示例性参考文献，实际引用时需通过PubMed、Web of Science等平台核实具体文献信息及原文内容。
F8 recombinant protein, also known as recombinant coagulation factor VIII (rFVIII), is a bioengineered therapeutic protein developed to treat hemophilia A, a genetic bleeding disorder caused by deficient or dysfunctional endogenous factor VIII. Hemophilia A affects approximately 1 in 5.000 males globally, leading to impaired blood clotting and spontaneous bleeding into joints, muscles, or organs.
Historically, factor VIII replacement therapy relied on plasma-derived products from human donors. However, these carried risks of pathogen transmission (e.g., HIV, hepatitis viruses) and inconsistent supply. The cloning of the F8 gene in 1984 enabled the development of recombinant FVIII, first approved by the FDA in 1992. This innovation eliminated reliance on human plasma, significantly improving safety and scalability.
Recombinant FVIII is produced using mammalian cell cultures (typically Chinese hamster ovary or baby hamster kidney cells) engineered to express the human F8 gene. The protein undergoes post-translational modifications to ensure functional similarity to natural factor VIII. Over decades, advancements have led to multiple generations of rFVIII products: first-generation versions contained human/animal protein stabilizers, while newer iterations use albumin-free formulations or chemical modifications to enhance stability and reduce immunogenicity.
Clinically, rFVIII is administered intravenously to prevent or treat bleeding episodes, enabling hemophilia A patients to maintain near-normal coagulation capacity. Prophylactic regimens have revolutionized care, reducing arthropathy and improving quality of life. Challenges persist, including the development of neutralizing antibodies (inhibitors) in ~30% of severe hemophilia patients, driving research into engineered FVIII variants with reduced immunogenicity.
Recent developments focus on extended half-life rFVIII products through PEGylation or Fc-fusion technologies, which decrease infusion frequency. Meanwhile, gene therapy approaches targeting durable F8 expression represent a potential paradigm shift toward functional cures. Despite these advances, accessibility remains uneven globally due to high costs, underscoring ongoing needs for affordable biosimilars and equitable distribution strategies.
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