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P8010L, Factor Xa Protease - 250 µg
2.258,03 RON
Factor Xa cleaves after the arginine residue in its preferred cleavage site Ile-Glu/Asp-Gly-Arg.
SKU
NEB_P8010L
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. 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Xa at secondary sites; this may indicate that these proteins are in a partially unfolded state (Walker, I., Riggs, P., unpublished observations).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.
Compatible for use with the pMAL™ Protein Fusion and Purification System (NEB #E8200)
Allows for convenient removal of MBP by loading the MBP-fusion digest onto amylose resin and collecting your protein of interest in the flow through.
Product Source
Factor Xa Protease is purified from bovine plasma and activated by treatment with the activating enzyme from Russell's viper venom.
| Price | 1.897,50 RON (preturile sunt fara TVA) |
|---|---|
| Description |
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. 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Xa at secondary sites; this may indicate that these proteins are in a partially unfolded state (Walker, I., Riggs, P., unpublished observations).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. Compatible for use with the pMAL™ Protein Fusion and Purification System (NEB #E8200) Product Source |
