Human Coagulation Factor VII Antibody Summary
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.
Coagulation Factor VII in Human PBMCs. Coagulation Factor VII was detected in immersion fixed PHA-stimulated human peripheral blood mononuclear cells (PBMCs) using 25 µg/mL Mouse Anti-Human Coagulation Factor VII Monoclonal Antibody (Catalog # MAB2338) for 3 hours at room temperature. Cells were stained (red) and counterstained (green). View our protocol for Fluorescent ICC Staining of Non-adherent Cells.
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 (aa 1 to 38), the mature chain can be further processed into the light chain (aa 39 to 190) and the heavy chain (aa 191 to 444).
- 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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