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The generation of the recombinant human coagulation factor IX (F9) protein begins with the co-cloning of the coagulation factor IX gene fragment (144-239aa) with the N-terminal 6xHis-GST tag gene into a vector. The constructed vectors are transformed into E.coli cells, which are induced with IPTG to express the recombinant protein. After cell lysis, Ni-NTA affinity chromatography is employed to purify the protein by exploiting the affinity between the 6xHis tag and nickel ions. The purified coagulation factor IX protein is then subjected to SDS-PAGE analysis to assess its purity, which consistently exceeds 85%. Human coagulation factor IX (FIX/F9) is a crucial vitamin K-dependent plasma protein that plays a significant role in the intrinsic pathway of blood coagulation. It is primarily synthesized in the liver and is essential for the conversion of factor X to its active form FXa, in the presence of calcium ions and phospholipids, which is a critical step in the coagulation cascade [1]. Deficiencies or mutations in the FIX gene lead to hemophilia B, an X-linked bleeding disorder characterized by recurrent spontaneous bleeding episodes [2][3]. The structure of FIX consists of a light chain and a heavy chain, connected by a linker region, which is vital for its function [4]. The activity of FIX is tightly regulated, and its deficiency can result in severe clinical manifestations, including hemarthrosis and internal bleeding, which can be life-threatening [5]. Recent advancements in gene therapy have shown promise for treating hemophilia B by restoring FIX levels. For instance, studies utilizing CRISPR/Cas9 technology have successfully knocked in human FIX into the swine F9 locus, demonstrating significant therapeutic effects in hemophilia B models [1]. References:[1] J. Chen, B. An, B. Yu, X. Peng, H. Yuan, Q. Yang, et al. Crispr/cas9-mediated knockin of human factor ix into swine factor ix locus effectively alleviates bleeding in hemophilia b pigs, Haematologica, vol. 106, no. 3, p. 829-837, 2020. https://doi.org/10.3324/haematol.2019.224063[2] R. Nigam, R. Choudhary, R. Malik, S. Kothari, K. Verma, A. Shrivastavae, et al. Clinicohematological study of hemophilia patients in bhopal, Journal of Evolution of Medical and Dental Sciences, vol. 3, no. 11, p. 2910-2916, 2014. https://doi.org/10.14260/jemds/2014/2224[3] L. Ramos-Petersen, A qualitative study exploring the experiences and perceptions of patients with hemophilia regarding their health-related well-being, in salamanca, Journal of Clinical Medicine, vol. 12, no. 16, p. 5417, 2023. https://doi.org/10.3390/jcm12165417[4] H. Kitano, A. Mamiya, T. Ishikawa, S. Kokubun, & C. Hidai, Coagulation factor ix regulates cell migration and adhesion in vitro, Cell Biology International, vol. 39, no. 10, p. 1162-1172, 2015. https://doi.org/10.1002/cbin.10491[5] K. Ohashi, K. Tatsumi, R. Utoh, S. Takagi, M. Shima, & T. Okano, Engineering liver tissues under the kidney capsule site provides therapeutic effects to hemophilia b mice, Cell Transplantation, vol. 19, no. 6-7, p. 807-813, 2010. https://doi.org/10.3727/096368910x508924
The generation of the recombinant human coagulation factor IX (F9) protein begins with the co-cloning of the coagulation factor IX gene fragment (144-239aa) with the N-terminal 6xHis-GST tag gene into a vector. The constructed vectors are transformed into E.coli cells, which are induced with IPTG to express the recombinant protein. After cell lysis, Ni-NTA affinity chromatography is employed to purify the protein by exploiting the affinity between the 6xHis tag and nickel ions. The purified coagulation factor IX protein is then subjected to SDS-PAGE analysis to assess its purity, which consistently exceeds 85%.
Human coagulation factor IX (FIX/F9) is a crucial vitamin K-dependent plasma protein that plays a significant role in the intrinsic pathway of blood coagulation. It is primarily synthesized in the liver and is essential for the conversion of factor X to its active form FXa, in the presence of calcium ions and phospholipids, which is a critical step in the coagulation cascade [1]. Deficiencies or mutations in the FIX gene lead to hemophilia B, an X-linked bleeding disorder characterized by recurrent spontaneous bleeding episodes [2][3].
The structure of FIX consists of a light chain and a heavy chain, connected by a linker region, which is vital for its function [4]. The activity of FIX is tightly regulated, and its deficiency can result in severe clinical manifestations, including hemarthrosis and internal bleeding, which can be life-threatening [5]. Recent advancements in gene therapy have shown promise for treating hemophilia B by restoring FIX levels. For instance, studies utilizing CRISPR/Cas9 technology have successfully knocked in human FIX into the swine F9 locus, demonstrating significant therapeutic effects in hemophilia B models [1].
References:[1] J. Chen, B. An, B. Yu, X. Peng, H. Yuan, Q. Yang, et al. Crispr/cas9-mediated knockin of human factor ix into swine factor ix locus effectively alleviates bleeding in hemophilia b pigs, Haematologica, vol. 106, no. 3, p. 829-837, 2020. https://doi.org/10.3324/haematol.2019.224063[2] R. Nigam, R. Choudhary, R. Malik, S. Kothari, K. Verma, A. Shrivastavae, et al. Clinicohematological study of hemophilia patients in bhopal, Journal of Evolution of Medical and Dental Sciences, vol. 3, no. 11, p. 2910-2916, 2014. https://doi.org/10.14260/jemds/2014/2224[3] L. Ramos-Petersen, A qualitative study exploring the experiences and perceptions of patients with hemophilia regarding their health-related well-being, in salamanca, Journal of Clinical Medicine, vol. 12, no. 16, p. 5417, 2023. https://doi.org/10.3390/jcm12165417[4] H. Kitano, A. Mamiya, T. Ishikawa, S. Kokubun, & C. Hidai, Coagulation factor ix regulates cell migration and adhesion in vitro, Cell Biology International, vol. 39, no. 10, p. 1162-1172, 2015. https://doi.org/10.1002/cbin.10491[5] K. Ohashi, K. Tatsumi, R. Utoh, S. Takagi, M. Shima, & T. Okano, Engineering liver tissues under the kidney capsule site provides therapeutic effects to hemophilia b mice, Cell Transplantation, vol. 19, no. 6-7, p. 807-813, 2010. https://doi.org/10.3727/096368910×508924
| Cat.No | ACP01466 | Target Name | F9 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 144-239aa | Mol Weight | 42.0 kDa |
| Protein Length | Partial | Purity | Greater than 85% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P00740 |
|---|
Uniprot Id
P00740
Target Species
Human
Target Name
F9
Target Full Name
Coagulation factor IX
Target Function
Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
Target Involvement
Hemophilia B (HEMB); Thrombophilia, X-linked, due to factor IX defect (THPH8)
Target Subcellular Location
Secreted.
Target Protein Families
Peptidase S1 family
Target Tissue Specificity
Detected in blood plasma (at protein level). Synthesized primarily in the liver and secreted in plasma.
Target Research Area
Cardiovascular
Target Synonyms
Christmas Disease; Christmas factor; Coagulant factor IX; Coagulation factor 9; Coagulation factor IX; Coagulation factor IXa heavy chain; F9; FA9_HUMAN; Factor 9; Factor IX Deficiency; FactorIX; FIX; Haemophilia B; HEMB; MGC129641; MGC129642; P19; Plasma Thromboplastic Component; Plasma thromboplastin component; PTC
Target Background
This gene encodes vitamin K-dependent coagulation factor IX that circulates in the blood as an inactive zymogen. This factor is converted to an active form by factor XIa, which excises the activation peptide and thus generates a heavy chain and a light chain held together by one or more disulfide bonds. The role of this activated factor IX in the blood coagulation cascade is to activate factor X to its active form through interactions with Ca+2 ions, membrane phospholipids, and factor VIII. Alterations of this gene, including point mutations, insertions and deletions, cause factor IX deficiency, which is a recessive X-linked disorder, also called hemophilia B or Christmas disease. Alternative splicing results in multiple transcript variants encoding different isoforms that may undergo similar proteolytic processing.
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