V8250
Snake venom from Echis carinatus
Synonym(s):
Saw-scaled Viper
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About This Item
Recommended Products
Quality Level
application(s)
metabolomics
vitamins, nutraceuticals, and natural products
storage temp.
−20°C
Application
Snake venom from Echis carinatus (Indian saw-scaled viper) which acts primarily on fibrinogen may be used as a source of anticoagulation factors and the prothrombin activator ecarin. It may also be used as an immunogen.
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Danger
hcodes
Hazard Classifications
Acute Tox. 2 Dermal - Acute Tox. 2 Oral
Storage Class
6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Effects of snake venom proteases on human fibrinogen chains.
Blood, 8, 120-125 (2010)
Toxicon : official journal of the International Society on Toxinology, 50(7), 893-900 (2007-08-08)
High titer antibodies (IgY) were raised in egg yolk of white leghorn chicken (Gallus gallus domesticus) by immunizing with the venom of Echis carinatus (Saw scaled viper or carpet viper), an Indian venomous snake belonging to the family Viperidae. The
Isolation and partial purification of anticoagulant fractions , from the venom of the Iranian snake Echis carinatus.
Bioengineered (2012)
Xenobiotica; the fate of foreign compounds in biological systems, 45(8), 663-671 (2015-02-13)
1. The safety, tolerability, pharmacokinetics, pharmacodynamics, and food effect of LB30870, a new selective thrombin inhibitor, were studied in 16 healthy men. 2. A double-blind, placebo-controlled single ascending dose study was done at oral doses of 5, 15, 30, 60, 120, and
Biochemistry, 57(18), 2694-2703 (2018-04-11)
Thrombin normally cleaves fibrinogen to promote coagulation; however, binding of thrombomodulin to thrombin switches the specificity of thrombin toward protein C, triggering the anticoagulation pathway. The W215A thrombin mutant was reported to have decreased activity toward fibrinogen without significant loss
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