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品質等級
儲存溫度
−20°C
應用
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.
生化／生理作用
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.
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, type N95 (US)
Snake venom proteins: development into antimicrobial and wound healing agents
PerumalSamy R, et al.
Mini-Reviews in Organic Chemistry, 11(1), 4-14 (2014)
beta-RTX. A receptor-active protein from Russell's viper (Vipera russelli russelli) venom.
Bevan P and Hiestand P
The Journal of Biological Chemistry, 258(8), 5319-5326 (1983)
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)
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)
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)
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