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About This Item
CAS Number:
UNSPSC Code:
12352204
MDL number:
NACRES:
NA.78
Specific activity:
20 units/mg protein
form
lyophilized powder
specific activity
20 units/mg protein
storage temp.
−20°C
Application
Factor V activating enzyme from Russell′s viper venom (RVV) is a single-chain glycoprotein that is involved in the rapid clotting of blood. Factor V circulates in the blood as an inactive cofactor and must be activated by proteases such as Factor V activating enzyme from RVV . This product may be useful in studying the blood coagulation cascade as well as the inherited deficiency called parahemophilia .
Biochem/physiol Actions
Factor V activator for RVV contains fucose, mannose, galactose, glucosamine, and neuraminic acid. Factor V activating enzyme from RVV is an arginine esterase that is sensitive to diisopropyl fluorophosphate (DFP) .
Physical form
Stabilized in albumin and sodium chloride.
Other Notes
One unit will increase the Factor V activity in 0.1 mL of fresh normal human plasma by at least 2× after incubation for 3 min at 37 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Kenneth Segers et al.
Proteins, 64(4), 968-984 (2006-06-30)
Blood coagulation factor V (FV) is a multifunctional protein that circulates in human plasma as a precursor molecule which can be activated by thrombin or activated factor X (FXa) in order to express its cofactor activity in prothrombin activation. FV
Laura M Haynes et al.
Arteriosclerosis, thrombosis, and vascular biology, 32(12), 2877-2883 (2012-10-02)
Rivaroxaban is an oral anticoagulant that directly targets both free factor Xa and factor Xa in complex with its protein cofactor, factor Va, in the prothrombinase complex. It is approved in the United States for the prophylaxis of deep vein
Rinku Majumder et al.
The Journal of biological chemistry, 286(41), 35535-35542 (2011-08-24)
Constituents of platelet membranes regulate the activity of the prothrombinase complex. We demonstrate that membranes containing phosphatidylcholine and phosphatidylethanolamine (PE) bind factor Va with high affinity (K(d) = ∼10 nm) in the absence of phosphatidylserine (PS). These membranes support formation
Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders.
W H Kane et al.
Blood, 71(3), 539-555 (1988-03-01)
Snake venom proteases that activate blood-coagulation factor V.
W Kisiel et al.
Methods in enzymology, 80 Pt C, 275-285 (1981-01-01)
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