Factor V Polyclonal Antibody
Affinity’s Factor V Polyclonal Antibody is the base level of our Factor V antibody family. The purity of IgG is typically 90% and is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v). The titre is essentially the same as the starting antiserum and each vial typically contains the amount of IgG recovered from one milliliter of antiserum. This Factor V Polyclonal Antibody is generally intended for use in applications such as immuno-precipitation, immuno-electrophoresis, immuno-depletion and activity neutralization assays.
Product Code: SAFV-IG
Retail Product Size: 10mg vial
Host Animal: Sheep Anti-Human Factor V Polyclonal Antibody
Species Cross Reactivity: View Chart
Product Datasheet: Factor V F5 Polyclonal Antibody - purified anti-human sheep IgG
Description of Factor V
Factor V (formerly referred to as accelerator globulin and labile factor) is a large glycoprotein (320 kDa) that is produced in the liver. The gene that encodes factor V (F5) is located on chromosome 1. A congenital deficiency of F5 is a hemorrhagic disorder inherited as an autosomal recessive disease. The concentration of F5 in plasma is typically 10 μg/mL. F5 is a pro-cofactor that is activated through limited proteolysis by thrombin, or by activated factor X in the presence of phospholipid surface. Other physiologic activators of FV include plasmin, neutrophil elastase and platelet calpain. The activated cofactor (FVa) is an essential component of the prothrombin activator complex, which consists of FVa, activated factor X, calcium and anionic phospholipid surface. The intact prothrombinase complex activates prothrombin to thrombin at a rate 300,000-fold greater than activated factor X alone. In a positive feedback loop, the thrombin generated accelerates its own generation by activating more FV to FVa. Thrombin also acts to down-regulate FVa indirectly by activating Protein C, which inactivates FVa cofactor activity1-3.
References and Reviews
1. Kane WH, Davie EW; Blood Coagulation Factors V and VIII: Structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders. Blood 71:539, 1988.
2. Hoyer, LW, Wyshock EG, Colman RW, in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 109-133, J.B. Lippincott Co., Philadelphia, 1994.
3. Nesheim ME, Katzmann JA, Tracy PB, Mann KG; in Methods in Enzymology 80:249, 1980.