TFPI Human, Sf9
Sf9, Baculovirus cells.
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
Greater than 90.0% as determined by SDS-PAGE.
Description
TFPI Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 285 amino acids (29-304a.a.) and having a molecular mass of 33kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TFPI is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Tissue Factor Pathway Inhibitor (Lipoprotein-Associated Coagulation Inhibitor), Extrinsic Pathway Inhibitor, Tissue Factor Pathway Inhibitor, anti-convertin, TFPI1, EPI, LACI, TFI.
Sf9, Baculovirus cells.
ADPDSEEDEE HTIITDTELP PLKLMHSFCA FKADDGPCKA IMKRFFFNIF TRQCEEFIYG GCEGNQNRFE SLEECKKMCT RDNANRIIKT TLQQEKPDFC FLEEDPGICR GYITRYFYNN QTKQCERFKY GGCLGNMNNF ETLEECKNIC EDGPNGFQVD NYGTQLNAVN NSLTPQSTKV PSLFEFHGPS WCLTPADRGL CRANENRFYY NSVIGKCRPF KYSGCGGNEN NFTSKQECLR ACKKGFIQRI SKGGLIKTKR KRKKQRVKIA YEEIFVKNMH HHHHH.
Product Science Overview
Tissue Factor Pathway Inhibitor (TFPI) is a crucial protein in the regulation of blood coagulation. It is a multivalent Kunitz-type serine protease inhibitor that plays a significant role in inhibiting the tissue factor (TF)-initiated blood coagulation cascade. The recombinant form of TFPI, produced in Sf9 insect cells, has been developed to study its structure, function, and therapeutic potential.
TFPI consists of three tandem Kunitz-type inhibitor domains. The first Kunitz domain (K1) inhibits factor VIIa/TF complex, while the second Kunitz domain (K2) inhibits factor Xa. The third Kunitz domain (K3) has a less defined role but is believed to contribute to the overall stability and function of the protein .
The primary function of TFPI is to regulate the extrinsic pathway of blood coagulation. It achieves this by forming a quaternary complex with factor VIIa/TF and factor Xa, thereby inhibiting the generation of thrombin and subsequent clot formation .
The recombinant production of TFPI in Sf9 insect cells involves the use of baculovirus expression systems. Sf9 cells, derived from the fall armyworm Spodoptera frugiperda, are commonly used for the production of recombinant proteins due to their high expression levels and ability to perform post-translational modifications similar to those in mammalian cells.
The process begins with the insertion of the TFPI gene into a baculovirus vector, which is then used to infect Sf9 cells. The infected cells produce the recombinant TFPI protein, which can be harvested and purified for further study and therapeutic use.
TFPI has shown promise as a therapeutic agent in the treatment of various coagulation disorders, including hemophilia. Hemophilia is a genetic disorder characterized by the deficiency of clotting factors, leading to excessive bleeding. Traditional treatments involve the replacement of the missing clotting factors, but these treatments can be expensive and have limitations.
Anti-TFPI therapies, including monoclonal antibodies and aptamers, have been investigated as potential treatments for hemophilia. By inhibiting TFPI, these therapies aim to restore thrombin generation and improve hemostasis in patients with hemophilia .
