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Catalog Number:

bs-0910P

Species:

Agkistrodon halys

AA Seq:

Purified native protein

Activity:

Not tested

Endotoxin:

Not analyzed

Storage:

Stored at -70℃ or -20℃. Avoid repeated freeze/thaw cycles.

Background:

Batroxobin is a protein of the serine protease family. Batroxobin is closely related in physiological function and molecular size to thrombin. Five subspecies for the Brazilian lancehead snake (Bothrops atrox) are found. Batroxobin obtained from certain subspecies exhibits the hemostatic efficacy, whereas the protein obtained from other subspecies exhibits the cleavage of fibrinogen. Some of the forms have hemostatic efficacy as main effect, where the other forms have degradation of fibrinogen as main effect. Batroxobin that is naturally extracted from the snake venom is mainly obtained from the snake Bothrops moojeni. Theoretically, the molecular weight of batroxobin should be around 25.5 kDa. Often, isolated batroxobin is heavier, around 33 kDa. The higher molecular weight is caused by a glycosylation modification during the secretion. The differences in weight result from different possible purification procedures, which can remove different sugar(chains) from the enzyme.