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V2501

Sigma-Aldrich

Snake venom from Vipera russelli (Russell′s Viper)

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About This Item

UNSPSC Code:
12352202

storage temp.

−20°C

Quality Level

Application

Snake venom from Vipera russelli (Russell′s Viper) has also been used as a positive control in indirect and sandwich enzyme-linked immunosorbent assay (ELISA) to study the performance of the immunochromatographic test (ICT)-Viper in venom detection in vitro and the detection of clinical envenoming, respectively.
Snake venom from Vipera russelli (Russell′s Viper) has been used for extraction of coagulant protein for complex generation with bovine X factor.

Biochem/physiol Actions

Snake venom can impose death on humans and animals. Nevertheless, snake venom also exhibits anti-bacterial and wound healing properties. Therefore, it is used as a therapeutic for treating various diseases including thrombosis, arthritis, and cancer.
Snake venom from Russell′s Viper is rich in toxins and proteinase inhibitors. The receptor from Vipera russelli β-RTX, interacts with monoamines and opiate and prevents their interaction with native receptors. The proteases from Russell′s Viper mediate coagulation in human plasma. The neurotoxicity of the venom is contributed by phospholipases.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Interaction of lanthanide ions with bovine factor X and their use in the affinity chromatography of the venom coagulant protein of Vipera russelli.
Furie BC and Furie B
The Journal of Biological Chemistry, 250(2), 601-608 (1975)
Snake venom proteins: development into antimicrobial and wound healing agents
PerumalSamy R, et al.
Mini-Reviews in Organic Chemistry, 11(1), 4-14 (2014)
Coagulation factor X activating enzyme from Russell's viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains.
Takeya H, et al.
The Journal of Biological Chemistry, 267(20), 14109-14117 (1992)
Snake Venom Proteinase Inhibitors: II. Chemical Structure of Inhibitor II Isolated from the Venom of Russell's viper (Vipera russelli)
TAKAHASHI H, et al.
Journal of Biochemistry, 76(4), 721-733 (1974)
Characterization and molecular cloning of neurotoxic phospholipases A2 from Taiwan viper (Vipera russelli formosensis)
WANG YM, et al.
European Journal of Biochemistry, 209(2), 635-641 (1992)

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