Recombinant Coagulation Factor IX is a purified Factor IX glycoprotein produced by recombinant DNA technology. It has a primary amino acid sequence that is identical to the Ala148 allelic form of human factor IX, and has structural and functional characteristics similar to those of endogenous factor IX. It is not derived from human blood (unlike human Factor IX complex), and is instead produced by a genetically engineered Chinese hamster ovary (CHO) cell line that secretes recombinant Factor IX into cell medium that is then processed and purified for use as a pharmaceutical agent. Recombinant Factor IX is indicated for the control and prevention of bleeding episodes in adult and pediatric patients with congenital factor IX deficiency (Hemophilia B).
<0.001 EU per 1 μg of the protein by the LAL method
Coagulation Factor IX (Recombinant)
For treatment of hemophilia (Christmas disease).
Examples of Clinical Use:
Hemophilia (Christmas disease)
Binds vitamin K and factor VIIIa. Cleaves the Arg-Ile bond in factor X to form active factor Xa. Plays a key role in blood coagulation and clotting. Injections of factor IX are used to treat hemophilia B, which is sometimes called Christmas disease. AlphaNine is injected to increase plasma levels of Factor IX and can temporarily correct this coagulation defect. The activated partial thromboplastin time (aPTT) is prolonged in people with hemophilia B. Treatment with factor IX concentrate may normalize the aPTT by temporarily replacing the factor IX. The administration increases plasma levels of factor IX, and can temporarily correct the coagulation defect in these patients.
Mechanism of action:
Coagulation Factor IX is an important protein in the process of hemostasis and normal blood clotting as it plays a key role within the coagulation cascade. It is located within the blood plasma as a zymogen, an antecedent to enzymatic function, in its inactivated state. Factor IX is dependent on the presence of Vitamin K, and is activated to a serine protease by the function of Coagulation Factor XIa. Factor XIa cleaves the peptide bond associated with protein activation in Factor IX, leaving Factor IX with two exposed chains, a light chain and a heavy chain. These two chains are held together by several disulfide bonds that reinforce the structure of Factor IX's activated form. After being activated, Factor IX forms a complex with calcium ions, membrane phospholipids and Coagulation Factor VIII to activate Coagulation Factor X. The activation of Factor X then performs a similarly integral step in the blood coagulation cascade. The ultimate result of phenotypically normal coagulation factors is the creation of platelets for normal blood clotting.
Recombinant Human Coagulation Factor IX (F9) is a recombinant human coagulation factor IX produced by genetic engineering technology. It is a serine protease that plays an important role in the coagulation process of humans. Compared to natural F9, recombinant F9 is structurally more pure and consistent and does not contain any impurities that could trigger an immune response. Recombinant F9 is primarily used to treat hemophilia B, a genetic disorder in which the body fails to produce enough F9, leading to clotting disorders and bleeding. By using recombinant F9, the deficient F9 in the patient's body can be supplemented, thus achieving the purpose of treatment. The use of recombinant F9 has received extensive clinical validation and approval. In terms of safety, recombinant F9 has been validated by a number of clinical trials, and its safety and efficacy have been fully confirmed. In addition, the use of recombinant F9 has been approved by drug regulatory authorities in several countries, including the US Food and Drug Administration (FDA) and the European Medicines Agency (EMA). In conclusion, Recombinant Human Coagulation Factor IX (F9) is an important biological drug used in the treatment of coagulation disorders such as hemophilia B, which has a high purity and consistency, and its safety and effectiveness have been fully verified and recognized.
Action Mechanism of Human F9 Protein
Recombinant Human Coagulation Factor IX (F9) is a recombinant human coagulation factor IX produced by genetic engineering technology. Its mechanism of action is mainly through participating in the coagulation process. In the course of coagulation, F9 combines with the phospholipids on the surface of endothelial cells in the presence of Ca² +, forming the F9-phospholipid-Ca ² + complex. This complex further activates F10, making it an active F10 enzyme. The F10 enzyme reactivates F11, initiating the exogenous clotting pathway. Compared to natural F9, recombinant F9 is structurally more pure and consistent and does not contain any impurities that could trigger an immune response. Therefore, recombinant F9 has significant advantages in the treatment of clotting disorders such as hemophilia B. In conclusion, Recombinant Human Coagulation Factor IX (F9) functions by participating in the coagulation process, and its mechanism is similar to that of natural F9, but with higher purity and consistency, providing an important therapeutic means for the treatment of coagulation disorders such as hemophilia B.
Advantages and Disadvantages of Human F9 Protein
Recombinant F9 is structurally and functionally very similar to natural F9, so it can effectively promote clotting and has a high safety and efficacy profile. The production process of the reconstituted F9 is more standardized and controllable, so the quality and purity of the product are well guaranteed. The use of recombinant F9 has been widely clinically validated and approved, and its efficacy and safety are well established. However, recombinant F9 also has some disadvantages in clinical application: the price of recombinant F9 is relatively high, which brings a large economic burden to patients. Although the safety and efficacy of recombinant F9 are well established, there are still some potential risks and side effects, such as allergic reactions, thrombosis, etc. Recombinant F9 requires frequent injection, which brings great inconvenience and pain to patients. In conclusion, Recombinant Human Coagulation Factor IX (F9) has good efficacy and safety in clinical application, but there are some shortcomings that need to be further improved and perfected.
Pipeline Research of Human F9 Protein
At present, the research pipeline of Recombinant Human Coagulation Factor IX (F9) mainly focuses on improving its production process, improving its quality and purity, reducing production cost, and exploring new application fields. In terms of the production process, researchers are trying to improve the production efficiency and purity of recombinant F9 through genetic engineering technology optimization and improvement. For example, by using more efficient expression systems and optimizing production processes, the yield and purity of recombinant F9 can be increased, thereby reducing production costs. In terms of improving quality and purity, researchers are investigating how to further remove impurities and immunogenic substances in recombinant F9 to improve its quality and purity. In addition, by studying the molecular structure and function of F9, new potential mutants, and improved forms can be discovered to improve its stability and activity. In terms of reducing production costs, the researchers are exploring ways to reduce the production cost of recombinant F9 by using cheaper cell lines, optimizing cell culture conditions, and adopting large-scale production techniques. This will help make retooling F9 more accessible and affordable. In exploring new areas of application, the researchers are investigating the use of recombinant F9 in other clotting disorders. For example, in some rare clotting disorders, mutations in F9 can lead to severe clotting disorders, and the development of recombinant F9 products targeting these mutations could provide better treatment options for these patients. In conclusion, the Recombinant Human Coagulation Factor IX (F9) pipeline has broad development prospects and will provide patients with better treatment options and higher quality of life.
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