Batroxobin, Native Protein

Batroxobin, Native Protein

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Batroxobin, Native Protein, isolated from Bothrops atrox snake venom, has a molecular weight of approximately 43 kDa.

Originally extracted from the venom of Bothrops atrox snake, Batroxobin is a serine protease that reduces fibrinogen levels via selective cleavage of Arg-Gly bonds in fibrinogen alpha chains (FGA) to form fibrin and release fibrinopeptide A. Batroxobin is closely related in physiological function and molecular size to thrombin. Unlike thrombin, Batroxobin is not affected by heparin and hirudin.

In biotechnology research, batroxobin is commonly used for the investigation of the last phase of blood coagulation. Due to its heparin insensitivity it can detect fibrinogen polymerization disorders even in the presence of heparin.

Other Names

Thrombin-like enzyme batroxobin, EC:, BX, SVTLE, Bothrops atrox serine proteinase, Fibrinogen-clotting enzyme, Reptilase, Snake venom serine protease (SVSP), Venombin A, UniProtKB# P04971.


Purified from Bothrops atrox snake venom.


Sterile filtered white lyophilized (freeze-dried) powder. The Batroxobin protein was lyophilized from a concentrated (1 mg/ml) solution with no additives.

Biological Activity

100 BU (Batroxobin Units) per milligram.


It is recommended to reconstitute the lyophilized Batroxobin in sterile 18MΩ-cm H2O not less than 100 µg/ml or more than 10 mg/ml solutions.


Ships at ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized Batroxobin at 2-8°C. Do not freeze.


This product is intended for Laboratory Research Use Only. Not for use in diagnostic or therapeutic procedures. This product may not be used as a pharmaceutical or veterinary drug, agricultural product, or food additive.


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