Factor Xa cleaves after the arginine residue in its preferred cleavage site Ile-(Glu or Asp)-Gly-Arg. It will sometimes cleave at other basic residues, depending on the conformation of the protein substrate (1,2,3). The most common secondary site, among those that have been sequenced, is Gly-Arg. There seems to be a correlation between proteins that are unstable in
E.coli and those that are cleaved by Factor Xa at secondary sites; this may indicate that these proteins are in a partially unfolded state (Walker, I., Riggs, P., unpublished observations). Factor Xa will not cleave a site followed by proline or arginine.
Product Source
Factor Xa Protease is purified from bovine plasma and activated by treatment with the activating enzyme from Russell"s viper venom.
- This product is related to the following categories:
- Proteases Products
- This product can be used in the following applications:
- Fusion Protein Cleavage,
- Target Protein Insolubility ,
- Protein Purification,
- Protein Digestion,
Protein Expression
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