|Detection of Mouse Coagulation Factor VII by Western Blot. Western blot shows lysate of mouse placenta tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Mouse Coagulation Factor VII Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3305) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for Coagulation Factor VII at approximately 50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Coagulation Factors VII and VIIa refer to the pro and active forms of the same protease, respectively (1). Factor VII is synthesized in the liver and circulates in the plasma where it binds to tissue factor (TF), an integral membrane protein found in a variety of cell types. Upon binding of TF, factor VII is rapidly converted into VIIa. The resulting 1:1 complex of VIIa and TF initiates the coagulation pathway and has also important coagulation-independent functions such as angiogenesis (2). The cleavage and activation of Coagulation Factors VII, IX and X by VIIa:TF is phospholipid-dependent whereas the cleavage of small peptide substrates is not (1). The deduced amino acid sequence of mouse factor VII predicts a signal peptide (residues 1 to 24), propeptide (residues 25 to 41), and the mature chain that can be further processed into the light chain (residues 42 to 193) and the heavy chain (residues 194 to 446). The amino acid sequence of mouse Factor VII is 89%, 71%, 65% and 55% identical to that of rat, human/dog, chimpanzee and chicken.
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