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F3380

Sigma-Aldrich

Factor V Activating Enzyme from Russell′s viper venom

lyophilized powder, 20 units/mg protein

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204

form

lyophilized powder

Quality Level

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) .

Unit Definition

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.

Physical form

Stabilized in albumin and sodium chloride.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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E Siigur et al.
Biochimica et biophysica acta, 1429(1), 239-248 (1999-01-27)
A factor V activator (VLFVA) was separated from Vipera lebetina venom by gel filtration on Sephadex G-100 superfine, followed by chromatography on CM-cellulose and on heparin-agarose. This enzyme (VLFVA) with a molecular mass of 28.4 kDa, as determined by matrix
Bioengineered factor Xa as a potential new strategy for hemophilia therapy.
Rodney M Camire
Expert review of hematology, 5(2), 121-123 (2012-04-06)
W Kisiel
The Journal of biological chemistry, 254(23), 12230-12234 (1979-12-10)
The protease from Russell's viper venom that activates Factor V was purified by gel filtration on Sephadex G-150 and ion exchange column chromatography on sulfopropyl (SP)-Sephadex C-50. The purified enzyme is a glycoprotein containing 6% carbohydrate. It migrated as a
Maria Cristina Bravo et al.
BMC systems biology, 6, 45-45 (2012-05-23)
Because understanding of the inventory, connectivity and dynamics of the components characterizing the process of coagulation is relatively mature, it has become an attractive target for physiochemical modeling. Such models can potentially improve the design of therapeutics. The prothrombinase complex
The C-terminus of tissue factor pathway inhibitor α is required for its interaction with factors V and Va.
M Ndonwi et al.
Journal of thrombosis and haemostasis : JTH, 10(9), 1944-1946 (2012-06-29)

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