Human Coagulation Factor VII Antibody Summary
-4, -5, -7, -8, -9, -10, -11, -12, -13, -14, -15, -B1, rhHGFA, rhFactor X, rhFactor XI, rhThrombin, rhuPA, or rhPROC is observed.
Accession # NP_062562
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Coagulation Factor VII in HASMC Human Cells by Flow Cytometry. HASMC human aortic smooth muscle cells were stained with Mouse Anti-Human Coagulation Factor VII Monoclonal Antibody (Catalog # MAB23381, filled histogram) or isotype control antibody (Catalog # MAB0041, open histogram), followed by Phycoerythrin-conjugated Anti-Mouse IgG F(ab')2Secondary Antibody (Catalog # F0102B).
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Coagulation Factor VII
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 angiognesis (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 predominant splicing variant of Factor VII in normal liver corresponds to the 444 amino acid precursor (3, 4). After a signal peptide (residues 1-38), the mature chain can be further processed into the light chain (residues 39-190) and the heavy chain (residues 191-444). The purified rhFactor VII corresponds to the mature chain, which can be processed and activated by treatment with thermolysin and binding with rhTissue Factor (R&D Systems, Catalog # 2339-PA) under the conditions described above.
- Morrissey, J.H. (2004) in Handbook of Proteolytic Enzymes, Barrett, A.J. et al. eds. p. 1659.
- Versteeg, H.H. et al. (2003) Carcinogenesis 24:1009.
- Hagen, F.S. et al. (1986) Proc. Natl. Acad. Sci. USA 83:2412.
- O’Hara, P.J. et al. (1987) Proc. Natl. Acad. Sci. USA 84:5158.
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